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Conserved domains on  [gi|446083982|ref|WP_000161837|]
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MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase [Staphylococcus]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 3-234 3.06e-68

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05324:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 225  Bit Score: 209.40  E-value: 3.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEAL-KALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLaKSGPGTVILTARDVERGQAAVEKLraeglSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFgmvtnpetaeskvnSLA 156
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSL--------------TSA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 157 YCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNnsKHVSEGIKPIIQLATIDADG-PTGTFINGNGEMP 233
Cdd:cd05324  147 YGVSKAALNALTRILAKELkeTGIKVNACCPGWVKTDMGGGKAP--KTPEEGAETPVYLALLPPDGePTGKFFSDKKVVP 224


                 .
gi 446083982 234 W 234
Cdd:cd05324  225 W 225
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-234 3.06e-68

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 209.40  E-value: 3.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEAL-KALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLaKSGPGTVILTARDVERGQAAVEKLraeglSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFgmvtnpetaeskvnSLA 156
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSL--------------TSA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 157 YCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNnsKHVSEGIKPIIQLATIDADG-PTGTFINGNGEMP 233
Cdd:cd05324  147 YGVSKAALNALTRILAKELkeTGIKVNACCPGWVKTDMGGGKAP--KTPEEGAETPVYLALLPPDGePTGKFFSDKKVVP 224


                 .
gi 446083982 234 W 234
Cdd:cd05324  225 W 225
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-197 2.88e-46

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.38  E-value: 2.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982    3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGalggkALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   78 LINNAGISGqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAY 157
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGS----------AY 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446083982  158 CSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFS 197
Cdd:pfam00106 150 SASKAAVIGFTRSLALELAphGIRVNAVAPGGVDTDMTKELR 191
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-232 6.07e-45

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 150.32  E-value: 6.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRaaggrALAVAADVTDEAAVEALVAAAVAAFGRLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSLAY 157
Cdd:COG1028   87 LVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGS----------PGQAAY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 158 CSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNNSKHVSEGIK---------------PIIQLATIDADG 220
Cdd:COG1028  156 AASKAAVVGLTRSLALELapRGIRVNAVAPGPIDTPMTRALLGAEEVREALAAriplgrlgtpeevaaAVLFLASDAASY 235

                        250
                 ....*....|..
gi 446083982 221 PTGTFINGNGEM 232
Cdd:COG1028  236 ITGQVLAVDGGL 247
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-164 1.25e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 116.54  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASqklGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIP---GVELLELDVTDDASVQAAVDEVIARAGRIDVLVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIS--G---QFSTPskltprDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnslAY 157
Cdd:PRK06179  82 GVGlaGaaeESSIA------QAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVL---GFLPAPYMA-------LY 145


                 ....*..
gi 446083982 158 CSSKSAV 164
Cdd:PRK06179 146 AASKHAV 152
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 5-109 3.85e-07

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 48.63  E-value: 3.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982     5 VLITGGNKGLGYASAEALKALGY-KVYIGSRNDVRGQQASQKLG--------VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAeleaagarVTVVACDVADRDALAAVLAAIPAVEGPL 82

                           90       100       110
                   ....*....|....*....|....*....|....
gi 446083982    76 DILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFG 109
Cdd:smart00822  83 TGVIHAAGV-LDDGVLASLTPERFAAVLAPKAAG 115
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 6-101 1.14e-03

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 39.14  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982    6 LITGGNKGLGYASAEALKALGYKVYIGSRNDvrgQQASQKLGVHY----------VQLDVTSDYSVKNAYNMIAEKE--- 72
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRS---AAAASTLAAELnarrpnsavtCQADLSNSATLFSRCEAIIDACfra 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 446083982   73 -GRLDILINNAgiSGQFSTPskLTPRDVEE 101
Cdd:TIGR02685  82 fGRCDVLVNNA--SAFYPTP--LLRGDAGE 107
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-234 3.06e-68

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 209.40  E-value: 3.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEAL-KALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLaKSGPGTVILTARDVERGQAAVEKLraeglSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFgmvtnpetaeskvnSLA 156
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSL--------------TSA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 157 YCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNnsKHVSEGIKPIIQLATIDADG-PTGTFINGNGEMP 233
Cdd:cd05324  147 YGVSKAALNALTRILAKELkeTGIKVNACCPGWVKTDMGGGKAP--KTPEEGAETPVYLALLPPDGePTGKFFSDKKVVP 224


                 .
gi 446083982 234 W 234
Cdd:cd05324  225 W 225
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-210 1.31e-47

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 157.39  E-value: 1.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN--DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNpdKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAYCSS 160
Cdd:cd05374   81 NAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLG----------PYCAS 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446083982 161 KSAVTMLTLQYAKGL--PNMQINAADPGATNTdlvgDFSNNSKHVSEGIKPI 210
Cdd:cd05374  150 KAALEALSESLRLELapFGIKVTIIEPGPVRT----GFADNAAGSALEDPEI 197
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-197 2.88e-46

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.38  E-value: 2.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982    3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGalggkALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   78 LINNAGISGqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAY 157
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGS----------AY 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446083982  158 CSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFS 197
Cdd:pfam00106 150 SASKAAVIGFTRSLALELAphGIRVNAVAPGGVDTDMTKELR 191
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-232 6.07e-45

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 150.32  E-value: 6.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRaaggrALAVAADVTDEAAVEALVAAAVAAFGRLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSLAY 157
Cdd:COG1028   87 LVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGS----------PGQAAY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 158 CSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNNSKHVSEGIK---------------PIIQLATIDADG 220
Cdd:COG1028  156 AASKAAVVGLTRSLALELapRGIRVNAVAPGPIDTPMTRALLGAEEVREALAAriplgrlgtpeevaaAVLFLASDAASY 235

                        250
                 ....*....|..
gi 446083982 221 PTGTFINGNGEM 232
Cdd:COG1028  236 ITGQVLAVDGGL 247
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-192 7.38e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 150.40  E-value: 7.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraagaRVEVVALDVTDPDAVAALAEAVLARFGPI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvnsl 155
Cdd:COG0300   84 DVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGL---PGMA------- 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 156 AYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDL 192
Cdd:COG0300  153 AYAASKAALEGFSESLRAELAptGVRVTAVCPGPVDTPF 191
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-196 8.69e-45

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 149.74  E-value: 8.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQK----LGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIealgGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPETAeskvnslAYCSS 160
Cdd:cd05233   81 NAGIAR-PGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRP---LPGQA-------AYAAS 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 161 KSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDF 196
Cdd:cd05233  150 KAALEGLTRSLALELapYGIRVNAVAPGLVDTPMLAKL 187
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-198 2.30e-42

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 143.40  E-value: 2.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MT---KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:COG4221    1 MSdkgKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGgrALAVPLDVTDEAAVEAAVAAAVAEFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnsl 155
Cdd:COG4221   81 DVLVNNAGV-ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGA---------- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 156 AYCSSKSAVTMLTLQYAKGLPNMQINAA--DPGATNTDLVGDFSN 198
Cdd:COG4221  150 VYAATKAAVRGLSESLRAELRPTGIRVTviEPGAVDTEFLDSVFD 194
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 3-232 4.19e-41

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 141.21  E-value: 4.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-------VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKketgnakVEVIQLDLSSLASVRQFAEEFLARFPRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGIsgqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGL---GSFGMVTNPETAESKV 152
Cdd:cd05327   82 DILINNAGI---MAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhraGPIDFNDLDLENNKEY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 153 N-SLAYCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNNS-----------KHVSEGIKPIIQLATIDA 218
Cdd:cd05327  159 SpYKAYGQSKLANILFTRELARRLegTGVTVNALHPGVVRTELLRRNGSFFllykllrpflkKSPEQGAQTALYAATSPE 238

                        250
                 ....*....|....*
gi 446083982 219 D-GPTGTFINGNGEM 232
Cdd:cd05327  239 LeGVSGKYFSDCKIK 253
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 5-234 2.59e-40

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 138.20  E-value: 2.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYsvKNAYNMIAE--KEGRLDI 77
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGashsrLHILELDVTDEI--AESAEAVAErlGDAGLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvTNPETaeskvnSLAY 157
Cdd:cd05325   79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGD-NTSGG------WYSY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 158 CSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNNSKHVS-----EGIKPIIQLATIdadGPTGTFINGNG 230
Cdd:cd05325  152 RASKAALNMLTKSLAVELkrDGITVVSLHPGWVRTDMGGPFAKNKGPITpeesvAGLLKVIDNLNE---EDSGKFLDYDG 228


                 ....*
gi 446083982 231 -EMPW 234
Cdd:cd05325  229 tEIPW 233
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 3-169 4.76e-33

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 119.50  E-value: 4.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINN 81
Cdd:COG3967    6 NTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANpGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGISGQ--FSTPSKlTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAYCS 159
Cdd:COG3967   86 AGIMRAedLLDEAE-DLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTP----------TYSA 154

                        170
                 ....*....|
gi 446083982 160 SKSAVTMLTL 169
Cdd:COG3967  155 TKAALHSYTQ 164
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-164 1.25e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 116.54  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASqklGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIP---GVELLELDVTDDASVQAAVDEVIARAGRIDVLVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIS--G---QFSTPskltprDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnslAY 157
Cdd:PRK06179  82 GVGlaGaaeESSIA------QAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVL---GFLPAPYMA-------LY 145


                 ....*..
gi 446083982 158 CSSKSAV 164
Cdd:PRK06179 146 AASKHAV 152
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 11-201 4.12e-29

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 109.06  E-value: 4.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   11 NKGLGYASAEALKALGYKV---YIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNAGISGQ 87
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVvltDLNEALAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAPK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   88 FSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEksEQPVVVNVSSgLGSFGMVTNPEtaeskvnslAYCSSKSAVTM 166
Cdd:pfam13561  85 LKGPfLDTSREDFDRALDVNLYSLFLLAKAALPLMK--EGGSIVNLSS-IGAERVVPNYN---------AYGAAKAALEA 152

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446083982  167 LTLQYAK--GLPNMQINAADPGATNTDLVGDFSNNSK 201
Cdd:pfam13561 153 LTRYLAVelGPRGIRVNAISPGPIKTLAASGIPGFDE 189
PRK08264 PRK08264
SDR family oxidoreductase;
3-168 5.76e-28

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 106.13  E-value: 5.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALG-YKVYIGSRNDvrGQQASQKLGVHYVQLDVTSDYSVKNAynmiAEKEGRLDILINN 81
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDP--ESVTDLGPRVVPLQLDVTDPASVAAA----AEAASDVTILVNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGIsgqFSTPSKLTPRDVEEV---YQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnslAYC 158
Cdd:PRK08264  81 AGI---FRTGSLLLEGDEDALraeMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVL---SWVNFPNLG-------TYS 147

                        170
                 ....*....|
gi 446083982 159 SSKSAVTMLT 168
Cdd:PRK08264 148 ASKAAAWSLT 157
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-192 2.36e-27

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 105.05  E-value: 2.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEaaggrAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsgqfsTPSK-LTPRDVEE---VYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetAEskvN 153
Cdd:PRK12939  88 LVNNAGI-----TNSKsATELDIDTwdaVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWG-------AP---K 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 154 SLAYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDL 192
Cdd:PRK12939 153 LGAYVASKGAVIGMTRSLARelGGRGITVNAIAPGLTATEA 193
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 3-169 2.57e-27

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 104.31  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINN 81
Cdd:cd05370    6 NTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELpNIHTIVLDVGDAESVEALAEALLSEYPNLDILINN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGI--SGQFSTPsKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAYCS 159
Cdd:cd05370   86 AGIqrPIDLRDP-ASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANP----------VYCA 154

                        170
                 ....*....|
gi 446083982 160 SKSAVTMLTL 169
Cdd:cd05370  155 TKAALHSYTL 164
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 3-189 4.57e-27

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 103.98  E-value: 4.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRND---VRGQQASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEekaEEAQQLIEKEGVeaTAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsgQFSTPSKLTPR-DVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslA 156
Cdd:cd05347   86 LVNNAGI--IRRHPAEEFPEaEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVP----------A 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446083982 157 YCSSKSAVTMLTLQYAK--GLPNMQINAADPG--ATN 189
Cdd:cd05347  154 YAASKGGVAGLTKALATewARHGIQVNAIAPGyfATE 190
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-134 5.34e-27

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 104.66  E-value: 5.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNdVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARR-VDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISGQFStpskltprdVEEV------YQ--TNVFGIVRMMNTFVPLLEKSEQPVVVNVSS 134
Cdd:PRK06182  83 GYGSYGA---------IEDVpidearRQfeVNLFGAARLTQLVLPHMRAQRSGRIINISS 133
FabG-like PRK07231
SDR family oxidoreductase;
3-196 5.92e-27

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 103.76  E-value: 5.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILaggrAIAVAADVSDEADVEAAVAAALERFGSVDIL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPETAeskvnslAYC 158
Cdd:PRK07231  86 VNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVAS---TAGLRPRPGLG-------WYN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 159 SSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDF 196
Cdd:PRK07231 156 ASKGAVITLTKALAAELgpDKIRVNAVAPVVVETGLLEAF 195
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 5-191 2.47e-26

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 101.98  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGY--KVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd05367    2 IILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEELRpglrVTTVKADLSDAAGVEQLLEAIRKLDGERDLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQP-VVVNVSSGLGS---FGMVtnpetaeskvns 154
Cdd:cd05367   82 INNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKkTVVNVSSGAAVnpfKGWG------------ 149

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446083982 155 lAYCSSKSAVTMLTLQYAKGLPNMQINAADPGATNTD 191
Cdd:cd05367  150 -LYCSSKAARDMFFRVLAAEEPDVRVLSYAPGVVDTD 185
PRK07326 PRK07326
SDR family oxidoreductase;
3-200 3.42e-26

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 101.63  E-value: 3.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNnkgnVLGLAADVRDEADVQRAVDAIVAAFGGLDVL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQpVVVNVSSGLGsfgmvTNPETaeskvNSLAYC 158
Cdd:PRK07326  87 IANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGG-YIINISSLAG-----TNFFA-----GGAAYN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446083982 159 SSK------SAVTMLTLQYAkglpNMQINAADPGATNTdlvgDFSNNS 200
Cdd:PRK07326 155 ASKfglvgfSEAAMLDLRQY----GIKVSTIMPGSVAT----HFNGHT 194
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-194 5.58e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 101.92  E-value: 5.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRN--DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSeaARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGsfGMVTNPETAeskvnslAYC 158
Cdd:PRK06180  83 VNNAGY-GHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITS-MG--GLITMPGIG-------YYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 159 SSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVG 194
Cdd:PRK06180 152 GSKFALEGISESLAKEVApfGIHVTAVEPGSFRTDWAG 189
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-191 1.50e-25

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 99.85  E-value: 1.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRaaggeARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQFSTPsKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS--GL-GSFGMVtnpetaeskv 152
Cdd:PRK05653  84 DILVNNAGITRDALLP-RMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSvsGVtGNPGQT---------- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 153 nslAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTD 191
Cdd:PRK05653 153 ---NYSAAKAGVIGFTKALALELAsrGITVNAVAPGFIDTD 190
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-196 1.58e-25

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 100.15  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd05341    6 KVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGdaARFFHLDVTDEDGWTAVVDTAREAFGRLDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsgqfstpskLTPRDVEE--------VYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPETAeskv 152
Cdd:cd05341   86 NAGI---------LTGGTVETttleewrrLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSS---IEGLVGDPALA---- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446083982 153 nslAYCSSKSAVTMLT----LQYAKGLPNMQINAADPGATNTDLVGDF 196
Cdd:cd05341  150 ---AYNASKGAVRGLTksaaLECATQGYGIRVNSVHPGYIYTPMTDEL 194
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 3-167 2.71e-25

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 100.04  E-value: 2.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRG------QQASQKLgvHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPgakelrRVCSDRL--RTLQLDVTKPEQIKRAAQWVKEHVGEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 I--LINNAGISGqFSTPSKLTPRDV-EEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSGLGSfgmVTNPETAeskvn 153
Cdd:cd09805   79 LwgLVNNAGILG-FGGDEELLPMDDyRKCMEVNLFGTVEVTKAFLPLLRRA-KGRVVNVSSMGGR---VPFPAGG----- 148

                        170
                 ....*....|....
gi 446083982 154 slAYCSSKSAVTML 167
Cdd:cd09805  149 --AYCASKAAVEAF 160
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-201 2.80e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 99.15  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL----GVH--YVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEikeeGGDaiAVKADVSSEEDVENLVEQIVEKFGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpETAESkvns 154
Cdd:PRK05565  84 IDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIG-----ASCEV---- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446083982 155 lAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVGDFSNNSK 201
Cdd:PRK05565 154 -LYSASKGAVNAFTKALAKELAPSGIrvNAVAPGAIDTEMWSSFSEEDK 201
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 3-190 4.56e-25

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 98.48  E-value: 4.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG---------VHYVQLDVTSDYSVKNAYNMIAEKEG 73
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeanasgqkVSYISADLSDYEEVEQAFAQAVEKGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGIS--GQFSTpskLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetaesK 151
Cdd:cd08939   82 PPDLVVNCAGISipGLFED---LTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVG----------I 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 152 VNSLAYCSSKSAVTML--TLQYAKGLPNMQINAADPGATNT 190
Cdd:cd08939  149 YGYSAYCPSKFALRGLaeSLRQELKPYNIRVSVVYPPDTDT 189
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 3-210 5.50e-25

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 98.51  E-value: 5.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFpvkvlpLQLDVSDRESIEAALENLPEEFRDID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmvtnpetaESKVNSLA 156
Cdd:cd05346   81 ILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGR----------YPYAGGNV 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPNMQINAA--DPGATNTD--LV---GDfSNNSKHVSEGIKPI 210
Cdd:cd05346  151 YCATKAAVRQFSLNLRKDLIGTGIRVTniEPGLVETEfsLVrfhGD-KEKADKVYEGVEPL 210
PRK12826 PRK12826
SDR family oxidoreductase;
1-195 6.08e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 98.45  E-value: 6.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEaaggkARARQVDVRDRAALKAAVAAGVEDFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQfsTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmVTNPETAesKVNS 154
Cdd:PRK12826  85 DILVANAGIFPL--TPfAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSS-------VAGPRVG--YPGL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 155 LAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGD 195
Cdd:PRK12826 154 AHYAASKAGLVGFTRALALELAarNITVNSVHPGGVDTPMAGN 196
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-192 6.61e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 98.70  E-value: 6.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIsgQFSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmvtnpeTAESKVNSLAYCSSK 161
Cdd:PRK06463  88 GI--MYLMPfEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAG---------IGTAAEGTTFYAITK 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446083982 162 SAVTMLT--LQYAKGLPNMQINAADPGATNTDL 192
Cdd:PRK06463 157 AGIIILTrrLAFELGKYGIRVNAVAPGWVETDM 189
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 3-193 1.22e-24

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 97.76  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS-----QKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAElqainPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISG-QFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQP---VVVNVSSGLGSFGMVTNPetaeskvn 153
Cdd:cd05323   81 LINNAGILDeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGkggVIVNIGSVAGLYPAPQFP-------- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 154 slAYCSSKSAVTMLTLQYAKGLP---NMQINAADPGATNTDLV 193
Cdd:cd05323  153 --VYSASKHGVVGFTRSLADLLEyktGVRVNAICPGFTNTPLL 193
PRK06398 PRK06398
aldose dehydrogenase; Validated
 3-193 1.55e-24

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 97.60  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRgqqasqKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------YNDVDYFKVDVSNKEQVIKGIDYVISKYGRIDILVNNA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGSFgMVTNpetaeskvNSLAYCSSKS 162
Cdd:PRK06398  81 GIE-SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIAS-VQSF-AVTR--------NAAAYVTSKH 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 163 AVTMLT----LQYAkglPNMQINAADPGATNTDLV 193
Cdd:PRK06398 150 AVLGLTrsiaVDYA---PTIRCVAVCPGSIRTPLL 181
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-190 3.10e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 97.05  E-value: 3.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG---VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINN 81
Cdd:PRK12829  14 VLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPgakVTATVADVADPAQVERVFDTAVERFGGLDVLVNN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSE-QPVVVNVSSGLG--SFGMVTNpetaeskvnslaYC 158
Cdd:PRK12829  94 AGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAGrlGYPGRTP------------YA 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 159 SSKSAVTMLTLQYAKGLP--NMQINAADPGATNT 190
Cdd:PRK12829 162 ASKWAVVGLVKSLAIELGplGIRVNAILPGIVRG 195
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-207 4.58e-24

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 95.94  E-value: 4.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGY-KVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAynmiAEKEGRLDILI 79
Cdd:cd05354    4 KTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGdkVVPLRLDVTDPESIKAA----AAQAKDVDVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGIsgqFSTPSKLTPRDVEEVYQ---TNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnslA 156
Cdd:cd05354   80 NNAGV---LKPATLLEEGALEALKQemdVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVA---SLKNFPAMG-------T 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446083982 157 YCSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDL---VGDFSNNSKHVSEGI 207
Cdd:cd05354  147 YSASKSAAYSLTqgLRAELAAQGTLVLSVHPGPIDTRMaagAGGPKESPETVAEAV 202
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 3-232 1.23e-23

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 94.88  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN------DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQGANVVINYASseagaeALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPETAeskvnslA 156
Cdd:PRK05557  86 ILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMG---NPGQA-------N 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 157 YCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFSNnskHVSEGIKPIIQ----------------LATIDA 218
Cdd:PRK05557 155 YAASKAGVIGFTKSLARELAsrGITVNAVAPGFIETDMTDALPE---DVKEAILAQIPlgrlgqpeeiasavafLASDEA 231

                        250
                 ....*....|....
gi 446083982 219 DGPTGTFINGNGEM 232
Cdd:PRK05557 232 AYITGQTLHVNGGM 245
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 3-193 1.23e-23

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 95.61  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS----QKLGVHYV---QLDVTSDYSVKN-AYNMIAEKEgR 74
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAaeirRDTLNHEVivrHLDLASLKSIRAfAAEFLAEED-R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGIsgqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMV-TNPETAESKVN 153
Cdd:cd09807   81 LDVLINNAGV---MRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKInFDDLNSEKSYN 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 154 SL-AYCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLV 193
Cdd:cd09807  158 TGfAYCQSKLANVLFTRELARRLqgTGVTVNALHPGVVRTELG 200
PRK05693 PRK05693
SDR family oxidoreductase;
3-205 1.35e-23

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 95.63  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN--DVRGQQASqklGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKaeDVEALAAA---GFTAVQLDVNDGAALARLAEELEAEHGGLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGisgqFSTPSKLTPRDVEEV---YQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSGLGSfgMVTnPETAeskvnslAY 157
Cdd:PRK05693  79 NAG----YGAMGPLLDGGVEAMrrqFETNVFAVVGVTRALFPLLRRS-RGLVVNIGSVSGV--LVT-PFAG-------AY 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446083982 158 CSSKSAVTMLT----LQYAkglP-NMQINAADPGATNTdlvgDFSNNSKHVSE 205
Cdd:PRK05693 144 CASKAAVHALSdalrLELA---PfGVQVMEVQPGAIAS----QFASNASREAE 189
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-201 1.61e-23

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 98.00  E-value: 1.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPdhHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTPS-KLTPRDVEEVYQTNVFGIVRMMNTFVPL-LEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnslAYC 158
Cdd:PRK06484  86 NAGVTDPTMTATlDTTLEEFARLQAINLTGAYLVAREALRLmIEQGHGAAIVNVASGA---GLVALPKRT-------AYS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 159 SSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVGDFSNNSK 201
Cdd:PRK06484 156 ASKAAVISLTRSLACEWAAKGIrvNAVLPGYVRTQMVAELERAGK 200
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-193 6.53e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 93.47  E-value: 6.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINN 81
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGlVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGI--SGQFSTPSKLTPRDVEEVyqtNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSF---GMVTnpetaeskvnsla 156
Cdd:PRK07825  86 AGVmpVGPFLDEPDAVTRRILDV---NVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIpvpGMAT------------- 149

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPN--MQINAADPGATNTDLV 193
Cdd:PRK07825 150 YCASKHAVVGFTDAARLELRGtgVHVSVVLPSFVNTELI 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 3-213 9.39e-23

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 92.61  E-value: 9.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIkalggNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPetaeSKVNslaY 157
Cdd:cd05333   81 LVNNAGIT-RDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIG---NP----GQAN---Y 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446083982 158 CSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFSNNskhVSEGIKPIIQL 213
Cdd:cd05333  150 AASKAGVIGFTKSLAKELAsrGITVNAVAPGFIDTDMTDALPEK---VKEKILKQIPL 204
PRK06172 PRK06172
SDR family oxidoreductase;
3-192 1.10e-22

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 92.51  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQ---QASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK06172   8 KVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEetvALIREAGgeALFVACDVTRDAEVKALVEQTIAAYGRLDY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmvtnpETAESKVNslAY 157
Cdd:PRK06172  88 AFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAG--------LGAAPKMS--IY 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 158 CSSKSAVTMLT----LQYAKGlpNMQINAADPGATNTDL 192
Cdd:PRK06172 158 AASKHAVIGLTksaaIEYAKK--GIRVNAVCPAVIDTDM 194
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-190 1.80e-22

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 91.56  E-value: 1.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDvrgqQASQKLGVHYVQLDVTSDYSVknaynmIAEKEGRLDILIN 80
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQD----KPDLSGNFHFLQLDLSDDLEP------LFDWVPSVDILCN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS--GLGSFGmvtnpetaeskvNSLAYC 158
Cdd:PRK06550  74 TAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSiaSFVAGG------------GGAAYT 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 159 SSKSAVTMLTLQ----YAKGlpNMQINAADPGATNT 190
Cdd:PRK06550 142 ASKHALAGFTKQlaldYAKD--GIQVFGIAPGAVKT 175
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 3-191 4.58e-22

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 90.80  E-value: 4.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd05344    2 KVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELraggaGVLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGiSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAESKVNSLAY 157
Cdd:cd05344   82 LVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 158 csSKSavtmLTLQYAKGlpNMQINAADPGATNTD 191
Cdd:cd05344  161 --VKT----LSRELAPD--GVTVNSVLPGYIDTE 186
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 3-193 8.88e-22

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 90.20  E-value: 8.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN-----DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEK-EGRLD 76
Cdd:cd05329    7 KTALVTGGTKGIGYAIVEELAGLGAEVYTCARNqkeldECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHfGGKLN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISgqFSTPSKL-TPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmvtnpetaeSKVNSL 155
Cdd:cd05329   87 ILVNNAGTN--IRKEAKDyTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGV-----------IAVPSG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 156 A-YCSSKSAVTMLT----LQYAKGlpNMQINAADPGATNTDLV 193
Cdd:cd05329  154 ApYGATKGALNQLTrslaCEWAKD--NIRVNAVAPWVIATPLV 194
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 3-194 1.68e-21

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 88.72  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL--GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQEleGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsGQFSTPSKLTPRD-VEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSGLGSfgmvtNPETAESkvnslAYCS 159
Cdd:cd08929   81 NAGV-GVMKPVEELTPEEwRLVLDTNLTGAFYCIHKAAPALLRRG-GGTIVNVGSLAGK-----NAFKGGA-----AYNA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 160 SK------SAVTMLTLQYAkglpNMQINAADPGATNTDLVG 194
Cdd:cd08929  149 SKfgllglSEAAMLDLREA----NIRVVNVMPGSVDTGFAG 185
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 3-211 3.40e-21

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 88.54  E-value: 3.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG------VHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05352    9 KVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAkkygvkTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISgqfSTPSKL--TPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgMVTNPEtaeskvNS 154
Cdd:cd05352   89 ILIANAGIT---VHKPALdyTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGT--IVNRPQ------PQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446083982 155 LAYCSSKSAVTMLtlqyAKGL------PNMQINAADPGATNTDLVGdfsNNSKHVSEGIKPII 211
Cdd:cd05352  158 AAYNASKAAVIHL----AKSLavewakYFIRVNSISPGYIDTDLTD---FVDKELRKKWESYI 213
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-195 6.38e-21

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 87.44  E-value: 6.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEaygvkVVIATADVSDYEEVTAAIEQLKNELGSIDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPETAeskvnslAY 157
Cdd:PRK07666  88 LINNAGI-SKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKG---AAVTS-------AY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 158 CSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDLVGD 195
Cdd:PRK07666 157 SASKFGVLGLTesLMQEVRKHNIRVTALTPSTVATDMAVD 196
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-186 1.26e-20

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 87.15  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd08942    7 KIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSaygeCIAIPADLSSEEGIEALVARVAERSDRLDVL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGIS-----GQFstPSKltprDVEEVYQTNVFGIVRMMNTFVPLLEKS---EQPV-VVNVSSGLGSFGmvtnpetae 149
Cdd:cd08942   87 VNNAGATwgaplEAF--PES----GWDKVMDINVKSVFFLTQALLPLLRAAataENPArVINIGSIAGIVV--------- 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 150 SKVNSLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPG 186
Cdd:cd08942  152 SGLENYSYGASKAAVHQLTRKLAKELAGEHItvNAIAPG 190
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-192 1.69e-20

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 86.26  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN--DVRGQQASQKlGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNpeDLAALSASGG-DVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTPSkLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfGMVTNPETaeskvnslAYCSS 160
Cdd:cd08932   80 NAGIGRPTTLRE-GSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSG--KRVLAGNA--------GYSAS 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 161 KSAVTMLTLQYAKGLPNMQINAAD--PGATNTDL 192
Cdd:cd08932  149 KFALRALAHALRQEGWDHGVRVSAvcPGFVDTPM 182
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 6-225 2.58e-20

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 86.49  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQA---------SQKLGVHYVqlDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd09808    5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEArkeietesgNQNIFLHIV--DMSDPKQVWEFVEEFKEEGKKLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGIsgqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGlgsfGMVT---NPETAESKVN 153
Cdd:cd09808   83 VLINNAGC---MVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSG----GMLVqklNTNNLQSERT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 154 ----SLAYCSSKSAVTMLTLQYAKGLPNMQINAADPGATNT--------DLVGDFSNNSKHVSEGIKPIIQLATIDA--D 219
Cdd:cd09808  156 afdgTMVYAQNKRQQVIMTEQWAKKHPEIHFSVMHPGWADTpavrnsmpDFHARFKDRLRSEEQGADTVVWLALSSAaaK 235


                 ....*.
gi 446083982 220 GPTGTF 225
Cdd:cd09808  236 APSGRF 241
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-190 2.93e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 88.75  E-value: 2.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY--VQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHlsVQADITDEAAVESAFAQIQARWGRLDVLVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEqpVVVNVSSGLGSFGMvtnpetaeskVNSLAYCSS 160
Cdd:PRK06484 350 NAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGG--VIVNLGSIASLLAL----------PPRNAYCAS 417

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446083982 161 KSAVTMLTLQYAKGLP--NMQINAADPGATNT 190
Cdd:PRK06484 418 KAAVTMLSRSLACEWApaGIRVNTVAPGYIET 449
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-234 4.24e-20

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 85.69  E-value: 4.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL------GVHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAvealgrRAQAVQADVTDKAALEAAVAAAVERFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGQFSTPsKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPETAeskvns 154
Cdd:PRK12825  85 IDILVNNAGIFEDKPLA-DMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPG---WPGRS------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 155 lAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVG---DFSNNSKHVSEGIKPIIQ----------LATIDAD 219
Cdd:PRK12825 155 -NYAAAKAGLVGLTKALARELAeyGITVNMVAPGDIDTDMKEatiEEAREAKDAETPLGRSGTpediaravafLCSDASD 233

                        250
                 ....*....|....*
gi 446083982 220 GPTGTFINGNGEMPW 234
Cdd:PRK12825 234 YITGQVIEVTGGVDV 248
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-210 4.50e-20

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 85.89  E-value: 4.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL------GVHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEiseagyNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGqfSTP-SKLTPRDVEEVYQTNVFGIVRMM----NTFVPLLEKSEqpvVVNVSSGLGSFGmvtNPETAe 149
Cdd:cd05366   81 FDVMVNNAGIAP--ITPlLTITEEDLKKVYAVNVFGVLFGIqaaaRQFKKLGHGGK---IINASSIAGVQG---FPNLG- 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446083982 150 skvnslAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVgdFSNNSKHVSEGIKPI 210
Cdd:cd05366  152 ------AYSASKFAVRGLTQTAAQELApkGITVNAYAPGIVKTEMW--DYIDEEVGEIAGKPE 206
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-190 5.41e-20

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 85.59  E-value: 5.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEAL---KALGYKVYIGSRNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIaeKEG 73
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLWEAAGALAggtletLQLDVCDSKSVAAAVERV--TER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAESKVN 153
Cdd:cd09806   79 HVDVLVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFA 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446083982 154 SLAYCSSksaVTMLTLQYakglpNMQINAADPGATNT 190
Cdd:cd09806  158 LEGLCES---LAVQLLPF-----NVHLSLIECGPVHT 186
PRK08267 PRK08267
SDR family oxidoreductase;
2-201 7.73e-20

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 84.99  E-value: 7.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG---VHYVQLDVTSDYSVKNAYNMIAEKE-GRLDI 77
Cdd:PRK08267   1 MKSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGagnAWTGALDVTDRAAWDAALADFAAATgGRLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGI--SGQFSTpskLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvnsl 155
Cdd:PRK08267  81 LFNNAGIlrGGPFED---IPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQ---PGLA------- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446083982 156 AYCSSKSAVTMLT----LQYAK-GlpnmqINAAD--PGATNTDLVGDFSNNSK 201
Cdd:PRK08267 148 VYSATKFAVRGLTealdLEWRRhG-----IRVADvmPLFVDTAMLDGTSNEVD 195
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 4-194 8.19e-20

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 84.93  E-value: 8.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS---QKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAaaiQQAGgqAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPetaeskvNSLAYC 158
Cdd:cd05365   81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISS---MSSENKNV-------RIAAYG 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 159 SSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDLVG 194
Cdd:cd05365  151 SSKAAVNHMTrnLAFDLGPKGIRVNAVAPGAVKTDALA 188
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 4-196 8.40e-20

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 84.85  E-value: 8.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKVyIGSrnDVRgqQAsqklgvhYVQLDVTSDYSVKNAYNMIAEK-EGRLDILINNA 82
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAGHTV-IGI--DLR--EA-------DVIADLSTPEGRAAAIADVLARcSGVLDGLVNCA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISGQFSTpskltprdvEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAES------------ 150
Cdd:cd05328   69 GVGGTTVA---------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDKLELAKAlaagtearaval 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446083982 151 -----KVNSLAYCSSKSAVTMLTLQ------YAKGLpnmQINAADPGATNTDLVGDF 196
Cdd:cd05328  140 aehagQPGYLAYAGSKEALTVWTRRraatwlYGAGV---RVNTVAPGPVETPILQAF 193
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-186 9.68e-20

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 84.69  E-value: 9.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYknrviaLELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGqFSTPSKLTPRDVEEVYQT---NVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFG----MVTNPet 147
Cdd:cd08930   81 IDILINNAYPSP-KVWGSRFEEFPYEQWNEVlnvNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIApdfrIYENT-- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 148 aeSKVNSLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPG 186
Cdd:cd08930  158 --QMYSPVEYSVIKAGIIHLTKYLAKYYADTGIrvNAISPG 196
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-228 1.12e-19

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 84.43  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRN------DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSgndcakDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvns 154
Cdd:PRK12824  81 VDILVNNAGIT-RDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQT--------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 155 lAYCSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDLVGDFsnnSKHVSEGIK---PIIQLATIDADG--------P 221
Cdd:PRK12824 151 -NYSAAKAGMIGFTkaLASEGARYGITVNCIAPGYIATPMVEQM---GPEVLQSIVnqiPMKRLGTPEEIAaavaflvsE 226


                 ....*..
gi 446083982 222 TGTFING 228
Cdd:PRK12824 227 AAGFITG 233
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 3-192 1.22e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 84.40  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTAAETYGSVDIAFNNA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIS----GQFSTPSKLTPRDVEEVYQTNVFGIVRMMntfVPLLEKSEQPVVVNVSSGLGSFGMVTnpetaeskvNSLAYC 158
Cdd:PRK06057  88 GISppedDSILNTGLDAWQRVQDVNLTSVYLCCKAA---LPHMVRQGKGSIINTASFVAVMGSAT---------SQISYT 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 159 SSKSAVTMLT----LQYAKglPNMQINAADPGATNTDL 192
Cdd:PRK06057 156 ASKGGVLAMSrelgVQFAR--QGIRVNALCPGPVNTPL 191
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 3-192 1.44e-19

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 84.38  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQ---QASQKLGVHYVQL-----DVTSDYSVKNAYNMIAEKEGR 74
Cdd:cd05364    4 KVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEetrQSCLQAGVSEKKIllvvaDLTEEEGQDRIISTTLAKFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGqfstPSKLTPRDVEE---VYQTNVFGIVRMMNTFVPLLEKSEQPvVVNVSSglgsfgMVTNPETAesk 151
Cdd:cd05364   84 LDILVNNAGILA----KGGGEDQDIEEydkVMNLNLRAVIYLTKLAVPHLIKTKGE-IVNVSS------VAGGRSFP--- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 152 vNSLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDL 192
Cdd:cd05364  150 -GVLYYCISKAALDQFTRCTALELAPKGVrvNSVSPGVIVTGF 191
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 5-191 1.78e-19

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 83.94  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS----QKLGVH--YVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVaaeiEELGGKavVVRADVSQPQDVEEMFAAVKERFGRLDVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGiSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGSFGmvTNPetaeskvNSLAYC 158
Cdd:cd05359   81 VSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISS-LGSIR--ALP-------NYLAVG 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 159 SSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTD 191
Cdd:cd05359  150 TAKAALEALVRYLAVELGPRGIrvNAVSPGVIDTD 184
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 1-192 1.82e-19

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 83.88  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQ-ASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETvAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISGQFSTPSK-----LTPRDVEEVYQTNVFGIVRMMNTFVPLLEKS------EQPVVVNVSSgLGSFgmvtnpeta 148
Cdd:cd05371   81 NCAGIAVAAKTYNKkgqqpHSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTAS-VAAF--------- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446083982 149 ESKVNSLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDL 192
Cdd:cd05371  151 EGQIGQAAYSASKGGIVGMTLPIARDLAPQGIrvVTIAPGLFDTPL 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-190 2.09e-19

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 84.01  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY-----VQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGgkaiaVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGqfSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQ-PVVVNVSSGLGSFGmvtNPETAeskvn 153
Cdd:PRK08643  81 NVVVNNAGVAP--TTPiETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVG---NPELA----- 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 154 slAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNT 190
Cdd:PRK08643 151 --VYSSTKFAVRGLTQTAARDLASEGItvNAYAPGIVKT 187
PRK05650 PRK05650
SDR family oxidoreductase;
5-134 4.70e-19

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 83.17  E-value: 4.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGV-----HYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggdgFYQRCDVRDYSQLTALAQACEEKWGGIDVIV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446083982  80 NNAGI-SGQFStpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS 134
Cdd:PRK05650  83 NNAGVaSGGFF--EELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIAS 136
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-196 6.28e-19

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 82.44  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd05345    4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGeaAIAIQADVTKRADVEAMVEAALSKFGRLDIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmvtnpetaESKVNSLAYC 158
Cdd:cd05345   84 VNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGL----------RPRPGLTWYN 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 159 SSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDF 196
Cdd:cd05345  154 ASKGWVVTATKAMAVELAprNIRVNCLCPVAGETPLLSMF 193
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-164 8.19e-19

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 81.90  E-value: 8.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRkaggkVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGI-SGqfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetaeskVNSLA- 156
Cdd:cd05339   81 INNAGVvSG--KKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLIS-----------PAGLAd 147


                 ....*...
gi 446083982 157 YCSSKSAV 164
Cdd:cd05339  148 YCASKAAA 155
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-175 1.12e-18

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 81.98  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDvrGQQASQKLgvHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06171  10 KIIIVTGGSSGIGLAIVKELLANGANVVNADIHG--GDGQHENY--QFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIS------------GQFstpsKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmvtnpetaES 150
Cdd:PRK06171  86 GINiprllvdekdpaGKY----ELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGL----------EG 151

                        170       180
                 ....*....|....*....|....*
gi 446083982 151 KVNSLAYCSSKSAVTMLTLQYAKGL 175
Cdd:PRK06171 152 SEGQSCYAATKAALNSFTRSWAKEL 176
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 3-187 1.32e-18

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 81.48  E-value: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG------VHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05369    4 KVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISsatggrAHPIQCDVRDPEAVEAAVDETLKEFGKID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGisGQFSTPS-KLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQP-VVVNVSSGLGSFGMvtnPETAESKvns 154
Cdd:cd05369   84 ILINNAA--GNFLAPAeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGgSILNISATYAYTGS---PFQVHSA--- 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 155 laycSSKSAVTMLTLQYAK--GLPNMQINAADPGA 187
Cdd:cd05369  156 ----AAKAGVDALTRSLAVewGPYGIRVNAIAPGP 186
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-194 1.68e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 81.62  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGdrLLPLALDVTDRAAVFAAVETAVEHFGRLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS--GLGSFGMVTnpetaeskvnslA 156
Cdd:PRK08263  82 VNNAGY-GLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSigGISAFPMSG------------I 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPNMQINAA--DPGATNTDLVG 194
Cdd:PRK08263 149 YHASKWALEGMSEALAQEVAEFGIKVTlvEPGGYSTDWAG 188
PRK07832 PRK07832
SDR family oxidoreductase;
3-194 1.80e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 81.63  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG------VHYVQLDVtSDY-SVKNAYNMIAEKEGRL 75
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARalggtvPEHRALDI-SDYdAVAAFAADIHAAHGSM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvns 154
Cdd:PRK07832  80 DVVMNIAGISA-WGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGHLVNVSSAAGLVAL---PWHA------ 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 155 lAYCSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDLVG 194
Cdd:PRK07832 150 -AYSASKFGLRGLSevLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-190 2.06e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 81.00  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL---GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVpadALRIGGIDLVDPQAARRAVDEVNRQFGRLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGIsgqFS--TPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSF---GMVtnpetaeskvns 154
Cdd:PRK12828  88 NIAGA---FVwgTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKagpGMG------------ 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 155 lAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNT 190
Cdd:PRK12828 153 -AYAAAKAGVARLTEALAAELLdrGITVNAVLPSIIDT 189
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-193 2.90e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 81.61  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-------GVHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpgaDVTLQELDLTSLASVRAAADALRAAYPRI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGIsgqfSTPSKLTPRD-VEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSF-GMV----TNPETAE 149
Cdd:PRK06197  97 DLLINNAGV----MYTPKQTTADgFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHRIrAAIhfddLQWERRY 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446083982 150 SKVNslAYCSSKSAVTMLT--LQ---YAKGLPNMQInAADPGATNTDLV 193
Cdd:PRK06197 173 NRVA--AYGQSKLANLLFTyeLQrrlAAAGATTIAV-AAHPGVSNTELA 218
PRK09072 PRK09072
SDR family oxidoreductase;
3-164 3.21e-18

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 80.76  E-value: 3.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL----GVHYVQLDVTSDySVKNAYNMIAEKEGRLDIL 78
Cdd:PRK09072   6 KRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLpypgRHRWVVADLTSE-AGREAVLARAREMGGINVL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvnslAYC 158
Cdd:PRK09072  85 INNAGVN-HFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGY---PGYA-------SYC 153


                 ....*.
gi 446083982 159 SSKSAV 164
Cdd:PRK09072 154 ASKFAL 159
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-164 3.88e-18

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 80.32  E-value: 3.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG------VHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05332    4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLelgapsPHVVPLDMSDLEDAEQVVEEALKLFGGLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvnslA 156
Cdd:cd05332   84 ILINNAGIS-MRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGV---PFRT-------A 152


                 ....*...
gi 446083982 157 YCSSKSAV 164
Cdd:cd05332  153 YAASKHAL 160
PRK09242 PRK09242
SDR family oxidoreductase;
3-208 6.44e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 79.79  E-value: 6.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-------VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAeefpereVHGLAADVSDDEDRRAILDWVEDHWDGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQFSTpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS--GLGSFGmvtnpetaeskvN 153
Cdd:PRK09242  90 HILVNNAGGNIRKAA-IDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSvsGLTHVR------------S 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446083982 154 SLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVGDFSNNSKHVSEGIK 208
Cdd:PRK09242 157 GAPYGMTKAALLQMTRNLAVEWAEDGIrvNAVAPWYIRTPLTSGPLSDPDYYEQVIE 213
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-217 6.64e-18

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 79.50  E-value: 6.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeggKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPetaeskvNSLAY 157
Cdd:cd08934   84 LVNNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISS---VAGRVAVR-------NSAVY 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446083982 158 CSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDLVGDFSNN-SKHVSEG-IKPIIQLATID 217
Cdd:cd08934  153 NATKFGVNAFSegLRQEVTERGVRVVVIEPGTVDTELRDHITHTiTKEAYEErISTIRKLQAED 216
PRK06947 PRK06947
SDR family oxidoreductase;
1-192 7.86e-18

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 79.46  E-value: 7.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL----GVH--YVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAvraaGGRacVVAGDVANEADVIAMFDAVQSAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGivrmmntfvPLLEKSEQPVVVNVSSGlGSFGMVTNPETAESKVNS 154
Cdd:PRK06947  81 LDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLG---------AYLCAREAARRLSTDRG-GRGGAIVNVSSIASRLGS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446083982 155 ----LAYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDL 192
Cdd:PRK06947 151 pneyVDYAGSKGAVDTLTLGLAKelGPHGVRVNAVRPGLIETEI 194
PRK07201 PRK07201
SDR family oxidoreductase;
3-163 1.84e-17

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 80.77  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN-----DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNgealdELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTpSKLTPR--DVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSsglgSFGMVTN-PETAeskvns 154
Cdd:PRK07201 452 LVNNAGRSIRRSV-ENSTDRfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVS----SIGVQTNaPRFS------ 520


                 ....*....
gi 446083982 155 lAYCSSKSA 163
Cdd:PRK07201 521 -AYVASKAA 528
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
3-191 2.08e-17

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 78.53  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGpaAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsgqFSTPSKL--TPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSSGLGSFGmvtnpetaESKVnsLAY 157
Cdd:PRK07067  87 NAAL---FDMAPILdiSRDSYDRLFAVNVKGLFFLMQAVARhMVEQGRGGKIINMASQAGRRG--------EALV--SHY 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 158 CSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTD 191
Cdd:PRK07067 154 CATKAAVISYTQSAALALIRHGInvNAIAPGVVDTP 189
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-172 2.46e-17

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 80.27  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGgpdrALGVACDVTDEAAVQAAFEEAALAFGGVDI 501

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQfSTPSKLTPRDVEEVYQTNVFG-------IVRMMntfvpLLEKSEQPVVVNVSSGlgsfgmVTNPetaes 150
Cdd:PRK08324 502 VVSNAGIAIS-GPIEETSDEDWRRSFDVNATGhflvareAVRIM-----KAQGLGGSIVFIASKN------AVNP----- 564

                        170       180
                 ....*....|....*....|..
gi 446083982 151 KVNSLAYCSSKSAVTMLTLQYA 172
Cdd:PRK08324 565 GPNFGAYGAAKAAELHLVRQLA 586
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 3-208 3.42e-17

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 77.96  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL------GVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd08933   10 KVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELnragpgSCKFVPCDVTKEEDIKTLISVTVERFGRID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSGLGSFGmvtnpetaesKVNSLA 156
Cdd:cd08933   90 CLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS-QGNIINLSSLVGSIG----------QKQAAP 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446083982 157 YCSSKSAVTMLTLQYA--KGLPNMQINAADPGATNTDLVGDFSNNSKHVSEGIK 208
Cdd:cd08933  159 YVATKGAITAMTKALAvdESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIK 212
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-191 3.75e-17

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 77.96  E-value: 3.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN--------DVRGQQASQKLGVhyvQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK06113  12 KCAIITGAGAGIGKEIAITFATAGASVVVSDINadaanhvvDEIQQLGGQAFAC---RCDITSEQELSALADFALSKLGK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGqfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmvtnpetaESK-VN 153
Cdd:PRK06113  89 VDILVNNAGGGG--PKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAA-----------ENKnIN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 154 SLAYCSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTD 191
Cdd:PRK06113 156 MTSYASSKAAASHLVrnMAFDLGEKNIRVNGIAPGAILTD 195
PRK06138 PRK06138
SDR family oxidoreductase;
3-192 3.76e-17

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 77.88  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL---GVHYV-QLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIaagGRAFArQGDVGSAEAVEALVDFVAARWGRLDVL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmvtnpeTAESKVNSlAYC 158
Cdd:PRK06138  86 VNNAGF-GCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLA---------LAGGRGRA-AYV 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 159 SSKSAVTMLT----LQYAKglPNMQINAADPGATNTDL 192
Cdd:PRK06138 155 ASKGAIASLTramaLDHAT--DGIRVNAVAPGTIDTPY 190
PRK06914 PRK06914
SDR family oxidoreductase;
1-192 4.40e-17

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 78.14  E-value: 4.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRN-------DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKeG 73
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNpekqenlLSQATQLNLQQNIKVQQLDVTDQNSIHNFQLVLKEI-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGIS-GQFstpskltprdVEEV--------YQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGM-VT 143
Cdd:PRK06914  81 RIDLLVNNAGYAnGGF----------VEEIpveeyrkqFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFpGL 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446083982 144 NPetaeskvnslaYCSSKSAVTMLTLQYAKGLPNMQINAA--DPGATNTDL 192
Cdd:PRK06914 151 SP-----------YVSSKYALEGFSESLRLELKPFGIDVAliEPGSYNTNI 190
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-192 5.24e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 77.31  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRND----VRGQQASQKLG--VHYVQLDVtSDYSVKNAYNMIAEKE-G 73
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDdeelAATQQELRALGveVIFFPADV-ADLSAHEAMLDAAQAAwG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGISgqfstPSK------LTPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPV-----VVNVSSglgSFGM 141
Cdd:PRK12745  80 RIDCLVNNAGVG-----VKVrgdlldLTPESFDRVLAINLRGPFFLTQAVAKrMLAQPEPEElphrsIVFVSS---VNAI 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446083982 142 VTNPETAEskvnslaYCSSKSAVTMLTLQYAKGLPNMQINAAD--PGATNTDL 192
Cdd:PRK12745 152 MVSPNRGE-------YCISKAGLSMAAQLFAARLAEEGIGVYEvrPGLIKTDM 197
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-192 5.33e-17

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 77.23  E-value: 5.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVyIG---SRNDVRGQQAsqklgvHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKV-IGfdqAFLTQEDYPF------ATFVLDVSDAAAVAQVCQRLLAETGPLDVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISGQFSTPSkLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmVTNPETAeskvnslAYCS 159
Cdd:PRK08220  82 NAAGILRMGATDS-LSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAH---VPRIGMA-------AYGA 150

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 160 SKSAVTMLTLQYAKGLP--NMQINAADPGATNTDL 192
Cdd:PRK08220 151 SKAALTSLAKCVGLELApyGVRCNVVSPGSTDTDM 185
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 3-195 5.36e-17

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 77.11  E-value: 5.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG---VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:cd05326    5 KVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGdpdISFVHCDVTVEADVRAAVDTAVARFGRLDIMF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISGQFSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetaesKVNSLAYC 158
Cdd:cd05326   85 NNAGVLGAPCYSiLETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVG----------GLGPHAYT 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 159 SSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGD 195
Cdd:cd05326  155 ASKHAVLGLTRSAATELGehGIRVNCVSPYGVATPLLTA 193
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-191 5.49e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 77.25  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNdvrgQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAGARVVTTARS----RPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDILVHVL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISgqfSTP----SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPETaeskvnSLAYC 158
Cdd:PRK06523  86 GGS---SAPaggfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTS---IQRRLPLPES------TTAYA 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 159 SSKSAVTmltlQYAKGLPN------MQINAADPGATNTD 191
Cdd:PRK06523 154 AAKAALS----TYSKSLSKevapkgVRVNTVSPGWIETE 188
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 3-201 6.54e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 77.36  E-value: 6.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK08265   7 KVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGerARFIATDITDDAAIERAVATVVARFGRVDILVN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTPSklTPRDVEEVYQTNVFGIVRMMNTFVPLLeKSEQPVVVNVSSGLGSFGmvtnpetaesKVNSLAYCSS 160
Cdd:PRK08265  87 LACTYLDDGLAS--SRADWLAALDVNLVSAAMLAQAAHPHL-ARGGGAIVNFTSISAKFA----------QTGRWLYPAS 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 161 KSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFSNNSK 201
Cdd:PRK08265 154 KAAIRQLTRSMAMDLApdGIRVNSVSPGWTWSRVMDELSGGDR 196
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 5-194 8.52e-17

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 76.74  E-value: 8.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVyIGSrnDVRGQQAsQKLGVHY--VQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATV-IAL--DLPFVLL-LEYGDPLrlTPLDVADAAAVREVCSRLLAEHGPIDALVNCA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISGQFSTPSkLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGlgsfgmvtnpETAESKVNSLAYCSSKS 162
Cdd:cd05331   77 GVLRPGATDP-LSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASN----------AAHVPRISMAAYGASKA 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 163 AVTMLTLQYAKGLP--NMQINAADPGATNTDLVG 194
Cdd:cd05331  146 ALASLSKCLGLELApyGVRCNVVSPGSTDTAMQR 179
PRK07856 PRK07856
SDR family oxidoreductase;
3-196 2.72e-16

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 75.36  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDvrGQQASQKlGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNA 82
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRA--PETVDGR-PAEFHAADVRDPDQVAALVDAIVERHGRLDVLVNNA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKseQP---VVVNVSSglgSFGMVTNPETAeskvnslAYCS 159
Cdd:PRK07856  84 GGS-PYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQ--QPgggSIVNIGS---VSGRRPSPGTA-------AYGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 160 SK----SAVTMLTLQYAkglPNMQINAADPGATNTDLVGDF 196
Cdd:PRK07856 151 AKagllNLTRSLAVEWA---PKVRVNAVVVGLVRTEQSELH 188
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 3-194 3.51e-16

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 75.08  E-value: 3.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd05348    5 EVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGdaVVGVEGDVRSLADNERAVARCVERFGKLDCFIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGI----SGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVS-SGLGSFGmvtnpetaeskvNSL 155
Cdd:cd05348   85 NAGIwdysTSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSnAGFYPGG------------GGP 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 156 AYCSSKSAVTMLTLQYAKGL-PNMQINAADPGATNTDLVG 194
Cdd:cd05348  153 LYTASKHAVVGLVKQLAYELaPHIRVNGVAPGGMVTDLRG 192
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-190 4.40e-16

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 74.43  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAynmiAEKEGRLDILINNA 82
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAAL----AKEEGRIDVLFNCA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GI--SGQFstpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVtnpetaeskVNSLAYCSS 160
Cdd:cd05368   79 GFvhHGSI---LDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGV---------PNRFVYSTT 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 161 KSAVTMLT----LQYA-KGLpnmQINAADPGATNT 190
Cdd:cd05368  147 KAAVIGLTksvaADFAqQGI---RCNAICPGTVDT 178
PRK07062 PRK07062
SDR family oxidoreductase;
3-136 4.64e-16

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 75.08  E-value: 4.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY-------VQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK07062   9 RVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFpgarllaARCDVLDEADVAAFAAAVEARFGGV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446083982  76 DILINNAGiSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGL 136
Cdd:PRK07062  89 DMLVNNAG-QGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLL 148
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-230 4.82e-16

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 74.73  E-value: 4.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNK--GLGYASAEALKALGYKVYI------------GSRND----VRGQQASQKLGVHYVQLDVTSDYSVK 62
Cdd:PRK12748   4 MKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFtywspydktmpwGMHDKepvlLKEEIESYGVRCEHMEIDLSQPYAPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  63 NAYNMIAEKEGRLDILINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSG--LGSFg 140
Cdd:PRK12748  84 RVFYAVSERLGDPSILINNAAYSTH-TRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGqsLGPM- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 141 mvtnpetaeskVNSLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVGDfsNNSKHVS------------EG 206
Cdd:PRK12748 162 -----------PDELAYAATKGAIEAFTKSLAPELAEKGItvNAVNPGPTDTGWITE--ELKHHLVpkfpqgrvgepvDA 228

                        250       260
                 ....*....|....*....|....
gi 446083982 207 IKPIIQLATIDADGPTGTFINGNG 230
Cdd:PRK12748 229 ARLIAFLVSEEAKWITGQVIHSEG 252
PRK06949 PRK06949
SDR family oxidoreductase;
3-192 5.32e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 74.80  E-value: 5.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMiAEKE-GRLD 76
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRrverlKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAH-AETEaGTID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGIsgqfSTPSKL---TPRDVEEVYQTNVFGIV--------RMMNTFVPLLEKSEQPVVVNVSS--GLGSFGMVT 143
Cdd:PRK06949  89 ILVNNSGV----STTQKLvdvTPADFDFVFDTNTRGAFfvaqevakRMIARAKGAGNTKPGGRIINIASvaGLRVLPQIG 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446083982 144 npetaeskvnslAYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDL 192
Cdd:PRK06949 165 ------------LYCMSKAAVVHMTRAMALewGRHGINVNAICPGYIDTEI 203
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-192 6.00e-16

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 74.86  E-value: 6.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGgepnVCFFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTP-RDVEEVYQTNVFGIVRMMN----TFVPlLEKSEQPVVVNVSSGLGSFGmvtnPEtaeskvn 153
Cdd:PLN02253  99 VNNAGLTGPPCPDIRNVElSEFEKVFDVNVKGVFLGMKhaarIMIP-LKKGSIVSLCSVASAIGGLG----PH------- 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 154 slAYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDL 192
Cdd:PLN02253 167 --AYTGSKHAVLGLTRSVAAelGKHGIRVNCVSPYAVPTAL 205
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 3-194 6.17e-16

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 74.61  E-value: 6.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGdhVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISgQFSTPSKLTPRDV-----EEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVS-SGLGSFGmvtnpetaeskvNS 154
Cdd:PRK06200  87 NAGIW-DYNTSLVDIPAETldtafDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSnSSFYPGG------------GG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 155 LAYCSSKSAVTMLTLQYAKGL-PNMQINAADPGATNTDLVG 194
Cdd:PRK06200 154 PLYTASKHAVVGLVRQLAYELaPKIRVNGVAPGGTVTDLRG 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 3-186 7.88e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 74.22  E-value: 7.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQK---LGVH--YVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07890   6 KVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEiddLGRRalAVPTDITDEDQCANLVALALERFGRVDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSglgsfgMVTNPetaeSKVNSLAY 157
Cdd:PRK07890  86 LVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMINS------MVLRH----SQPKYGAY 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446083982 158 CSSKSAVTMLTLQYAK--GLPNMQINAADPG 186
Cdd:PRK07890 155 KMAKGALLAASQSLATelGPQGIRVNSVAPG 185
PRK07454 PRK07454
SDR family oxidoreductase;
1-192 9.02e-16

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 73.84  E-value: 9.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRN-----DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK07454   5 SMPRALITGASSGIGKATALAFAKAGWDLALVARSqdaleALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISgqFSTPSKLTP-RDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS--GLGSFgmvtnPETAeskv 152
Cdd:PRK07454  85 DVLINNAGMA--YTGPLLEMPlSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSiaARNAF-----PQWG---- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 153 nslAYCSSKSAVTMLTLQYAKGLPNMQINAAD--PGATNTDL 192
Cdd:PRK07454 154 ---AYCVSKAALAAFTKCLAEEERSHGIRVCTitLGAVNTPL 192
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-193 1.09e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 73.60  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRG--------QQASQKLG-VHYVQLDVTSDYSVKNAYNMIAEK 71
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGraeadavaAGIEAAGGkALGLAFDVRDFAATRAALDAGVEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  72 EGRLDILINNAGISGQFSTPsKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQP-VVVNVSSGLGSFGmvtnpetaes 150
Cdd:PRK12827  85 FGRLDILVNNAGIATDAAFA-ELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGgRIVNIASVAGVRG---------- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 151 KVNSLAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLV 193
Cdd:PRK12827 154 NRGQVNYAASKAGLIGLTKTLANELAprGITVNAVAPGAINTPMA 198
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 3-193 1.10e-15

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 73.71  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-------GVHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapdaEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSL 155
Cdd:cd05330   84 DGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGV----------GNQS 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 156 AYCSSKSAVTMLT----LQYakGLPNMQINAADPGATNTDLV 193
Cdd:cd05330  154 GYAAAKHGVVGLTrnsaVEY--GQYGIRINAIAPGAILTPMV 193
PRK09291 PRK09291
SDR family oxidoreductase;
1-164 1.55e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 73.49  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYnmiaekEGRL 75
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQiapqvTALRAEAARRGLALRVEKLDLTDAIDRAQAA------EWDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGqfSTPSKLTPRD-VEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSSGlgsfGMVTNPETAeskvn 153
Cdd:PRK09291  75 DVLLNNAGIGE--AGAVVDIPVElVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMA----GLITGPFTG----- 143

                        170
                 ....*....|.
gi 446083982 154 slAYCSSKSAV 164
Cdd:PRK09291 144 --AYCASKHAL 152
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-192 2.06e-15

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 72.80  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRG-----QQASQKLGVHY-VQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05358    4 KVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAaeevvEEIKAVGGKAIaVQADVSKEEDVVALFQSAIKEFGTLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFStPSKLTPRDVEEVYQTNVFG--------IVRMMntfvpllEKSEQPVVVNVSSglgsfgmvtnpeta 148
Cdd:cd05358   84 ILVNNAGLQGDAS-SHEMTLEDWNKVIDVNLTGqflcareaIKRFR-------KSKIKGKIINMSS-------------- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446083982 149 eskVNSL-------AYCSSKSAVTMLT----LQYAKglPNMQINAADPGATNTDL 192
Cdd:cd05358  142 ---VHEKipwpghvNYAASKGGVKMMTktlaQEYAP--KGIRVNAIAPGAINTPI 191
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-192 2.77e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 72.44  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAynmiAEKEGRLDILINNA 82
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVGDDAAIRAA----LAAAGAFDGLVNCA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSLAYCSSK 161
Cdd:PRK07060  86 GIA-SLESALDMTAEGFDRVMAVNARGAALVARHVARaMIAAGRGGSIVNVSSQAALVGL----------PDHLAYCASK 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446083982 162 SAVTMLTLQYAK--GLPNMQINAADPGATNTDL 192
Cdd:PRK07060 155 AALDAITRVLCVelGPHGIRVNSVNPTVTLTPM 187
PRK08628 PRK08628
SDR family oxidoreductase;
3-172 4.27e-15

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 72.30  E-value: 4.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQ--QASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEfaEELRALQPraEFVQVDLTDDAQCRDAVEQTVAKFGRIDGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSklTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSglgsfgmvtnpETAES-KVNSLAY 157
Cdd:PRK08628  88 VNNAGVNDGVGLEA--GREAFVASLERNLIHYYVMAHYCLPHLKAS-RGAIVNISS-----------KTALTgQGGTSGY 153

                        170
                 ....*....|....*
gi 446083982 158 CSSKSAVTMLTLQYA 172
Cdd:PRK08628 154 AAAKGAQLALTREWA 168
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-230 4.38e-15

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 71.92  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKV---YIGSR---NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVvvnYASSKaaaEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQpvVVNVSSGLgsfgmvtnpeTAESKVNSLA 156
Cdd:cd05362   84 ILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGR--IINISSSL----------TAAYTPNYGA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVgdFSNNSKHVSEGIK---PIIQLATIDADGPTGTFINGNG 230
Cdd:cd05362  151 YAGSKAAVEAFTRVLAKELGGRGItvNAVAPGPVDTDMF--YAGKTEEAVEGYAkmsPLGRLGEPEDIAPVVAFLASPD 227
PRK06196 PRK06196
oxidoreductase; Provisional
 3-135 4.54e-15

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 72.79  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINN 81
Cdd:PRK06196  27 KTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIdGVEVVMLDLADLESVRAFAERFLDSGRRIDILINN 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446083982  82 AGIsgqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSG 135
Cdd:PRK06196 107 AGV---MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSA 157
PRK07069 PRK07069
short chain dehydrogenase; Validated
 6-168 5.92e-15

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 71.66  E-value: 5.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQA-------SQKLGVHY-VQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAfaaeinaAHGEGVAFaAVQDVTDEAQWQALLAQAADAMGGLSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPetaeskvNSLAY 157
Cdd:PRK07069  83 LVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISS---VAAFKAEP-------DYTAY 151

                        170
                 ....*....|.
gi 446083982 158 CSSKSAVTMLT 168
Cdd:PRK07069 152 NASKAAVASLT 162
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-186 7.50e-15

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 71.33  E-value: 7.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQA-SQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAvAAEAGerAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISGQFSTPSKLTPRDVE-EVYQTNVFGIVR----MMNTFVPLLEKSEQPVVVNVSSGLgsfgmVTNPetaesKVNS 154
Cdd:cd05349   81 NNALIDFPFDPDQRKTFDTIDwEDYQQQLEGAVKgalnLLQAVLPDFKERGSGRVINIGTNL-----FQNP-----VVPY 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 155 LAYCSSKSAVTMLTLQYAKGLP--NMQINAADPG 186
Cdd:cd05349  151 HDYTTAKAALLGFTRNMAKELGpyGITVNMVSGG 184
PRK08017 PRK08017
SDR family oxidoreductase;
1-164 8.08e-15

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 71.27  E-value: 8.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSR--NDVrgqQASQKLGVHYVQLDVTSDYSVKNAYN-MIAEKEGRLDI 77
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRkpDDV---ARMNSLGFTGILLDLDDPESVERAADeVIALTDNRLYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAG--ISGQFSTPSKltpRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnsl 155
Cdd:PRK08017  78 LFNNAGfgVYGPLSTISR---QQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVM---GLISTPGRG------- 144


                 ....*....
gi 446083982 156 AYCSSKSAV 164
Cdd:PRK08017 145 AYAASKYAL 153
PRK08177 PRK08177
SDR family oxidoreductase;
3-195 9.70e-15

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 70.44  E-value: 9.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKegRLDILINNA 82
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKLDMNDPASLDQLLQRLQGQ--RFDLLFVNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GISG-QFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKsEQPVVVNVSSGLGSfgmVTNPETAESKVnslaYCSSK 161
Cdd:PRK08177  80 GISGpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRP-GQGVLAFMSSQLGS---VELPDGGEMPL----YKASK 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 162 SAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGD 195
Cdd:PRK08177 152 AALNSMTRSFVAELgePTLTVLSMHPGWVKTDMGGD 187
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 3-192 1.05e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 70.95  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07523  11 RRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKgqglsAHALAFDVTDHDAVRAAIDAFEAEIGPIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsgQFSTPSKLTPRDV-EEVYQTNVFGIVRMmntfvplleksEQPVVVN-VSSGLGSFGMVTNPETAESKVNSL 155
Cdd:PRK07523  91 LVNNAGM--QFRTPLEDFPADAfERLLRTNISSVFYV-----------GQAVARHmIARGAGKIINIASVQSALARPGIA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 156 AYCSSKSAVTMLT----LQYAK-GLpnmQINAADPGATNTDL 192
Cdd:PRK07523 158 PYTATKGAVGNLTkgmaTDWAKhGL---QCNAIAPGYFDTPL 196
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-190 1.09e-14

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 70.92  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDV--RGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNwdETRRLIEKEGrkVTFVQVDLTKPESAEKVVKEALEEFGKIDIL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQfsTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAY 157
Cdd:PRK06935  96 VNNAGTIRR--APlLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVP----------AY 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 158 CSSKSAVTMLTLQYAKGLP--NMQINAADPGATNT 190
Cdd:PRK06935 164 TASKHGVAGLTKAFANELAayNIQVNAIAPGYIKT 198
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-201 1.13e-14

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 70.80  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQA-SQKLG-----VHYVQLDVTsdySVKNAYNMIAEKE---G 73
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENlVNELGkeghdVYAVQADVS---KVEDANRLVEEAVnhfG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAESKVN 153
Cdd:PRK12935  84 KVDILVNNAGIT-RDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446083982 154 SLAYCSSksavtmLTLQYAKglPNMQINAADPGATNTDLVGDFSNNSK 201
Cdd:PRK12935 163 MLGFTKS------LALELAK--TNVTVNAICPGFIDTEMVAEVPEEVR 202
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 3-168 1.21e-14

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 70.56  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG---VHYVQLDVTSDYSVKNAYNMIAEKEG-RLDIL 78
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaenVVAGALDVTDRAAWAAALADFAAATGgRLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGI--SGQFSTPSKltpRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvnslA 156
Cdd:cd08931   81 FNNAGVgrGGPFEDVPL---AAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQ---PDLA-------V 147

                        170
                 ....*....|..
gi 446083982 157 YCSSKSAVTMLT 168
Cdd:cd08931  148 YSATKFAVRGLT 159
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 3-190 1.47e-14

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 70.30  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGV--HYVQLDVTSDYSVKNAYNM------IAEKEGR 74
Cdd:cd05340    5 RIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEegGRQPQWFILDLLTCTSENCqqlaqrIAVNYPR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetaesKVNS 154
Cdd:cd05340   85 LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQG----------RANW 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 155 LAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNT 190
Cdd:cd05340  155 GAYAVSKFATEGL*QVLADEYQqrNLRVNCINPGGTRT 192
PRK07063 PRK07063
SDR family oxidoreductase;
3-198 2.72e-14

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 70.08  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-------VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIArdvagarVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmvtnpeTAESKV--N 153
Cdd:PRK07063  88 DVLVNNAGIN-VFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIAS------------THAFKIipG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446083982 154 SLAYCSSKSAVTMLT----LQYAKglPNMQINAADPGATNTDLVGDFSN 198
Cdd:PRK07063 155 CFPYPVAKHGLLGLTralgIEYAA--RNVRVNAIAPGYIETQLTEDWWN 201
PRK05993 PRK05993
SDR family oxidoreductase;
1-228 3.50e-14

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 70.06  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVrGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEK-EGRLDILI 79
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEE-DVAALEAEGLEAFQLDYAEPESIAALVAQVLELsGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNaGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpetaesKVNSlAYCS 159
Cdd:PRK05993  82 NN-GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPM---------KYRG-AYNA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 160 SKSAVT--MLTLQYAKGLPNMQINAADPGATNTdlvgDFSNNS-KHVSEGI---------KPIIQLATIDADGPTGTFIN 227
Cdd:PRK05993 151 SKFAIEglSLTLRMELQGSGIHVSLIEPGPIET----RFRANAlAAFKRWIdiensvhraAYQQQMARLEGGGSKSRFKL 226


                 .
gi 446083982 228 G 228
Cdd:PRK05993 227 G 227
PRK07814 PRK07814
SDR family oxidoreductase;
3-190 3.50e-14

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 69.81  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07814  11 QVAVVTGAGRGLGAAIALAFAEAGADVLIAARtesqlDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGqfstPSKL---TPRDVEEVYQTNVFGIVRMMNTFVPL-LEKSEQPVVVNVSSGLGSFgmvtnpetaeSKVN 153
Cdd:PRK07814  91 VVNNVGGTM----PNPLlstSTKDLADAFTFNVATAHALTVAAVPLmLEHSGGGSVINISSTMGRL----------AGRG 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 154 SLAYCSSKSAVTMLTLQYAKGL-PNMQINAADPGATNT 190
Cdd:PRK07814 157 FAAYGTAKAALAHYTRLAALDLcPRIRVNAIAPGSILT 194
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 3-189 4.24e-14

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 68.84  E-value: 4.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRND----VRGQQASQKLGVHY--VQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSeaeaQRLKDELNALRNSAvlVQADLSDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfGMVTNPETaeskvNSLA 156
Cdd:cd05357   81 VLVNNASAFYP-TPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIID-----AMTDRPLT-----GYFA 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 157 YCSSKSAVTMLTLQYAKGL-PNMQINAADPGATN 189
Cdd:cd05357  150 YCMSKAALEGLTRSAALELaPNIRVNGIAPGLIL 183
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
3-201 4.42e-14

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 69.33  E-value: 4.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDvrgQQASQKL------GVHYVQLDVTSDYSVKNAYNMI---AEKEG 73
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTE---NKELTKLaeqynsNLTFHSLDLQDVHELETNFNEIlssIQEDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDI-LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEK-SEQPVVVNVSSGLGSfgmvtNPETAESk 151
Cdd:PRK06924  79 VSSIhLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDwKVDKRVINISSGAAK-----NPYFGWS- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446083982 152 vnslAYCSSKSAVTMLTL-----QYAKGLPNmQINAADPGATNTDLVGDFSNNSK 201
Cdd:PRK06924 153 ----AYCSSKAGLDMFTQtvateQEEEEYPV-KIVAFSPGVMDTNMQAQIRSSSK 202
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 5-168 6.40e-14

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 68.51  E-value: 6.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRN-----DVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRtdrldELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISgqFSTPSKLTP-RDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAYC 158
Cdd:cd05350   81 INAGVG--KGTSLGDLSfKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAA----------AYS 148

                        170
                 ....*....|
gi 446083982 159 SSKSAVTMLT 168
Cdd:cd05350  149 ASKAALSSLA 158
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 2-187 7.48e-14

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 68.57  E-value: 7.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQK--LGVHY--VQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAaqGGPRAlgVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLL--EKSEQPVVVNVSSGlgsfgmVTNPetaesKVNSL 155
Cdd:cd08943   81 VVSNAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMksQGIGGNIVFNASKN------AVAP-----GPNAA 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 156 AYCSSKSAVTMLTLQYAK--GLPNMQINAADPGA 187
Cdd:cd08943  149 AYSAAKAAEAHLARCLALegGEDGIRVNTVNPDA 182
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-193 8.24e-14

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 68.63  E-value: 8.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYI---GSRNDVR----GQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEG 73
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLngfGDAAEIEavraGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGIsgQFSTPSKLTPRDV-EEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetaesKV 152
Cdd:cd08940   81 GVDILVNNAGI--QHVAPIEDFPTEKwDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVA----------SA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 153 NSLAYCSSKSAVTMLT----LQYAKglPNMQINAADPGATNTDLV 193
Cdd:cd08940  149 NKSAYVAAKHGVVGLTkvvaLETAG--TGVTCNAICPGWVLTPLV 191
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 3-186 1.19e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 68.05  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARkaeelEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISgqFSTPSKLTPRD-VEEVYQTNVFGIV--------RMMntfvpllEKSEQPVVVNVSS--GLGSfgmvTNPE 146
Cdd:PRK08213  93 LVNNAGAT--WGAPAEDHPVEaWDKVMNLNVRGLFllsqavakRSM-------IPRGYGRIINVASvaGLGG----NPPE 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 147 TaeskVNSLAYCSSKSAVTMLTLQYAK--GLPNMQINAADPG 186
Cdd:PRK08213 160 V----MDTIAYNTSKGAVINFTRALAAewGPHGIRVNAIAPG 197
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-195 1.19e-13

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 68.06  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGalgteVRGYAANVTDEEDVEATFAQIAEDFGQLNG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGI----------SGQFStpSKLTPRDVEEVYQTNVFGivrmmnTF-------VPLLEKSEQPVVVNVSS--GLGS 138
Cdd:PRK08217  86 LINNAGIlrdgllvkakDGKVT--SKMSLEQFQSVIDVNLTG------VFlcgreaaAKMIESGSKGVIINISSiaRAGN 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446083982 139 FGMvTNpetaeskvnslaYCSSKSAVTMLTLQYAKGLPNMQINAAD--PGATNTDLVGD 195
Cdd:PRK08217 158 MGQ-TN------------YSASKAGVAAMTVTWAKELARYGIRVAAiaPGVIETEMTAA 203
PRK06953 PRK06953
SDR family oxidoreductase;
3-194 1.37e-13

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 67.40  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVyIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKN-AYNMIAEkegRLDILINN 81
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRV-IATARDAAALAALQALGAEALALDVADPASVAGlAWKLDGE---ALDAAVYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGISG---QFSTPskLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSGLGSFGMVTNpetaeskVNSLAYC 158
Cdd:PRK06953  78 AGVYGprtEGVEP--ITREDFDAVMHTNVLGPMQLLPILLPLVEAA-GGVLAVLSSRMGSIGDATG-------TTGWLYR 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 159 SSKSAVTM----LTLQYakglPNMQINAADPGATNTDLVG 194
Cdd:PRK06953 148 ASKAALNDalraASLQA----RHATCIALHPGWVRTDMGG 183
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 3-192 1.59e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 67.76  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY--VQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06841  16 KVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAkgLVCDVSDSQSVEAAVAAVISAFGRIDILVN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSLAYCSS 160
Cdd:PRK06841  96 SAGV-ALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVAL----------ERHVAYCAS 164

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 161 KSAVTMLT----LQYAKglPNMQINAADPGATNTDL 192
Cdd:PRK06841 165 KAGVVGMTkvlaLEWGP--YGITVNAISPTVVLTEL 198
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-171 1.98e-13

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 67.24  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRN----DVRGQQASQKLGVH--YVQLDVTSDYSvknAYNMIAEKEGRLDI- 77
Cdd:cd05356    4 AVVTGATDGIGKAYAEELAKRGFNVILISRTqeklDAVAKEIEEKYGVEtkTIAADFSAGDD---IYERIEKELEGLDIg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 -LINNAGISgqFSTPSKLTPRDVEEVYQ---TNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvn 153
Cdd:cd05356   81 iLVNNVGIS--HSIPEYFLETPEDELQDiinVNVMATLKMTRLILPGMVKRKKGAIVNISSFA---GLIPTPLLA----- 150

                        170       180
                 ....*....|....*....|
gi 446083982 154 slAYCSSKSAVTMLT--LQY 171
Cdd:cd05356  151 --TYSASKAFLDFFSraLYE 168
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-191 2.17e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 67.34  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYK-VYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK06198   7 KVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELealgaKAVFVQADLSDVEDCRRVVAAADEAFGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQfSTPSKLTPRDVEEVYQTNV---F----GIVRMMntfvplLEKSEQPVVVNVSSglgSFGMVTNPETAe 149
Cdd:PRK06198  87 ALVNAAGLTDR-GTILDTSPELFDRHFAVNVrapFflmqEAIKLM------RRRKAEGTIVNIGS---MSAHGGQPFLA- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446083982 150 skvnslAYCSSKSAVTMLTLQYAKG-LPN-MQINAADPGATNTD 191
Cdd:PRK06198 156 ------AYCASKGALATLTRNAAYAlLRNrIRVNGLNIGWMATE 193
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 3-190 3.45e-13

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 66.83  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVH--YVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNlfFVHGDVADETLVKFVVYAMLEKLGRIDVLVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsgqfSTPSKLTPRDVEE---VYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSglgsfgmvtnPETAESKVNSLAY 157
Cdd:cd09761   82 NAAR----GSKGILSSLLLEEwdrILSVNLTGPYELSRYCRDELIKN-KGRIINIAS----------TRAFQSEPDSEAY 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 158 CSSKSAVTMLTLQYAKGL-PNMQINAADPGATNT 190
Cdd:cd09761  147 AASKGGLVALTHALAMSLgPDIRVNCISPGWINT 180
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-193 3.55e-13

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 66.75  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQL--DVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALrvDVTDEQQVAALFERAVEEFGGLDLLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPETAeskvnslAYCSS 160
Cdd:cd08944   84 NAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSG---DPGYG-------AYGAS 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 161 KSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLV 193
Cdd:cd08944  154 KAAIRNLTRTLAAELRHAGIrcNALAPGLIDTPLL 188
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 3-190 4.37e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 66.67  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQ----ASQKLGVH--YVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK08936   8 KVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANdvaeEIKKAGGEaiAVKGDVTVESDVVNLIQTAVKEFGTLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQfsTPSKLTPRD----VEEVYQTNVF-GIVRMMNTFVpllEKSEQPVVVNVSSglgSFGMVTNPETAEsk 151
Cdd:PRK08936  88 VMINNAGIENA--VPSHEMSLEdwnkVINTNLTGAFlGSREAIKYFV---EHDIKGNIINMSS---VHEQIPWPLFVH-- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 152 vnslaYCSSKSAVTMLT----LQYAKglPNMQINAADPGATNT 190
Cdd:PRK08936 158 -----YAASKGGVKLMTetlaMEYAP--KGIRVNNIGPGAINT 193
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 4-190 4.52e-13

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 66.25  E-value: 4.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKVYIGSRN---------DVRGQQASqklgVHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSaealhelarEVRELGGE----AIAVVADVADAAQVERAADTAVERFGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvns 154
Cdd:cd05360   78 IDTWVNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSA---PLQA------ 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 155 lAYCSSKSAVT----MLTLQYAKGLPNMQINAADPGATNT 190
Cdd:cd05360  148 -AYSASKHAVRgfteSLRAELAHDGAPISVTLVQPTAMNT 186
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-193 4.65e-13

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 66.70  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN-----DVRGQQASQKLGV-HYVQLDVTSDYSVKNAYNMIAEKE-GRL 75
Cdd:cd09763    4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqlPGTAEEIEARGGKcIPVRCDHSDDDEVEALFERVAREQqGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNA--GISGQFSTPSK----LTPRDVEEV--------YQTNVFGivrmmntfVPLLEKSEQPVVVNVSSGLGSFGM 141
Cdd:cd09763   84 DILVNNAyaAVQLILVGVAKpfweEPPTIWDDInnvglrahYACSVYA--------APLMVKAGKGLIVIISSTGGLEYL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446083982 142 VTnpetaeskvnsLAYCSSKSAVTMLTLQYAKGLPNMQINAAD--PGATNTDLV 193
Cdd:cd09763  156 FN-----------VAYGVGKAAIDRMAADMAHELKPHGVAVVSlwPGFVRTELV 198
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 6-195 4.89e-13

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 66.33  E-value: 4.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRND----VRGQQASQKLGVH--YVQLDVtSDYSVKNAY-NMIAEKEGRLDIL 78
Cdd:cd05337    5 IVTGASRGIGRAIATELAARGFDIAINDLPDddqaTEVVAEVLAAGRRaiYFQADI-GELSDHEALlDQAWEDFGRLDCL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISgqfSTPSK----LTPRDVEEVYQTNVFGIVRMMNTFVplLEKSEQPV--------VVNVSSglGSFGMVTnPE 146
Cdd:cd05337   84 VNNAGIA---VRPRGdlldLTEDSFDRLIAINLRGPFFLTQAVA--RRMVEQPDrfdgphrsIIFVTS--INAYLVS-PN 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446083982 147 TAEskvnslaYCSSKSAVTMLTLQYAKGLPNMQINAAD--PGATNTDLVGD 195
Cdd:cd05337  156 RGE-------YCISKAGLSMATRLLAYRLADEGIAVHEirPGLIHTDMTAP 199
PRK06124 PRK06124
SDR family oxidoreductase;
3-195 4.90e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 66.27  E-value: 4.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQA-----SQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAvaalrAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSLAY 157
Cdd:PRK06124  92 LVNNVGARDR-RPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVAR----------AGDAVY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446083982 158 CSSKSAVTMLTLQYAKGLPNMQI--NAADPGA----TNTDLVGD 195
Cdd:PRK06124 161 PAAKQGLTGLMRALAAEFGPHGItsNAIAPGYfateTNAAMAAD 204
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 3-96 4.99e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 66.24  E-value: 4.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEqfpgqVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81

                         90       100
                 ....*....|....*....|
gi 446083982  78 LINNAgiSGQFSTPS-KLTP 96
Cdd:PRK07677  82 LINNA--AGNFICPAeDLSV 99
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 3-192 6.78e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 65.93  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK08085  10 KNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRqegikAHAAPFNVTHKQEVEAAIEHIEKDIGPIDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIsgQFSTPSKLTPR----DVEEVYQTNVF----GIVRMMntfvpllEKSEQPVVVNVSSGLGSFGMVT-NPeta 148
Cdd:PRK08085  90 LINNAGI--QRRHPFTEFPEqewnDVIAVNQTAVFlvsqAVARYM-------VKRQAGKIINICSMQSELGRDTiTP--- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446083982 149 eskvnslaYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDL 192
Cdd:PRK08085 158 --------YAASKGAVKMLTRGMCVELArhNIQVNGIAPGYFKTEM 195
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 2-228 7.92e-13

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 65.53  E-value: 7.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALGYKVYIG-SRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIeaaggRAIAVQADVADAAAVTRLFDAAETAFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGqfstPSKLTPRDVE---EVYQTNVFGivrmmnTFVPLLEKSEQpvvvnvssgLGSFGMVTNPET---AE 149
Cdd:PRK12937  85 DVLVNNAGVMP----LGTIADFDLEdfdRTIATNLRG------AFVVLREAARH---------LGQGGRIINLSTsviAL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 150 SKVNSLAYCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLV--GDFSNNSKHVSeGIKPIIQLATIDA------- 218
Cdd:PRK12937 146 PLPGYGPYAASKAAVEGLVHVLANELrgRGITVNAVAPGPVATELFfnGKSAEQIDQLA-GLAPLERLGTPEEiaaavaf 224

                        250
                 ....*....|.
gi 446083982 219 -DGPTGTFING 228
Cdd:PRK12937 225 lAGPDGAWVNG 235
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 3-186 8.94e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 65.85  E-value: 8.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIgsrNDV------RGQQASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVF---NDInqelvdKGLAAYRELGIeaHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGISGQfsTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnpETAEskvn 153
Cdd:PRK07097  88 IDILVNNAGIIKR--IPmLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGR----ETVS---- 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 154 slAYCSSKSAVTMLTLQYAK--GLPNMQINAADPG 186
Cdd:PRK07097 158 --AYAAAKGGLKMLTKNIASeyGEANIQCNGIGPG 190
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-205 1.20e-12

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 65.24  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRND----VRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:cd08937    5 KVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSElvheVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDVL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGiSGQFSTPSKLTP-RDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmvtnpeTAESKVNSLAY 157
Cdd:cd08937   85 INNVG-GTIWAKPYEHYEeEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSS------------IATRGIYRIPY 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446083982 158 CSSKSAVTMLT--LQYAKGLPNMQINAADPGATNTDlVGDFSNNSKHVSE 205
Cdd:cd08937  152 SAAKGGVNALTasLAFEHARDGIRVNAVAPGGTEAP-PRKIPRNAAPMSE 200
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-84 1.34e-12

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 65.29  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaggKAIGVAMDVTDEEAINAGIDYAVETFGGVDI 84


                 ....*..
gi 446083982  78 LINNAGI 84
Cdd:PRK12429  85 LVNNAGI 91
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 3-199 1.37e-12

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 65.23  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN-----DVRGQ-QASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:cd05343    7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRvdkieALAAEcQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQGVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGIsGQFSTPSKLTPRDVEEVYQTNVfgivrmMNTFVPLLEKSEQPVVVNVSSG----LGSFGMVTNPETAESKV 152
Cdd:cd05343   87 VCINNAGL-ARPEPLLSGKTEGWKEMFDVNV------LALSICTREAYQSMKERNVDDGhiinINSMSGHRVPPVSVFHF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446083982 153 nslaYCSSKSAVTMLT------LQYAKglPNMQINAADPGATNTDLVGDFSNN 199
Cdd:cd05343  160 ----YAATKHAVTALTeglrqeLREAK--THIRATSISPGLVETEFAFKLHDN 206
PRK09730 PRK09730
SDR family oxidoreductase;
2-195 1.55e-12

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 64.87  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK09730   1 MAIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAggkafvLQADISDENQVVAMFTAIDQHDEPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGivrmmnTFVPLLEKSEQPVVVNVSSGlgsfGMVTNPETAESKVNS- 154
Cdd:PRK09730  81 AALVNNAGILFTQCTVENLTAERINRVLSTNVTG------YFLCCREAVKRMALKHGGSG----GAIVNVSSAASRLGAp 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446083982 155 ---LAYCSSKSAVTMLTlqyaKGLP------NMQINAADPGATNTDLVGD 195
Cdd:PRK09730 151 geyVDYAASKGAIDTLT----TGLSlevaaqGIRVNCVRPGFIYTEMHAS 196
PRK06181 PRK06181
SDR family oxidoreductase;
3-164 1.68e-12

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 65.00  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQ-----LDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEalvvpTDVSDAEACERLIEAAVARFGGIDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQfSTPSKLTPRDV-EEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVnVSSGLGSFGMVTNPetaeskvnslA 156
Cdd:PRK06181  82 LVNNAGITMW-SRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKASRGQIVV-VSSLAGLTGVPTRS----------G 149


                 ....*...
gi 446083982 157 YCSSKSAV 164
Cdd:PRK06181 150 YAASKHAL 157
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-200 1.93e-12

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 64.82  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY----VQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHrctaVVADVRDPASVAAAIKRAKEKEGRIDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGIS--GQFstpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgMVTNPETAeskvnslA 156
Cdd:PRK08226  87 VNNAGVCrlGSF---LDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGD--MVADPGET-------A 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446083982 157 YCSSKSAVTMLT----LQYAKGlpNMQINAADPGATNTDLVGDFSNNS 200
Cdd:PRK08226 155 YALTKAAIVGLTkslaVEYAQS--GIRVNAICPGYVRTPMAESIARQS 200
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-225 2.18e-12

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 64.34  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS---------------QKLGV--HYVQLDVTSDYSVKNAY 65
Cdd:cd05338    4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSakslpgtieetaeeiEAAGGqaLPIVVDVRDEDQVRALV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  66 NMIAEKEGRLDILINNAG---ISGQFSTPSKlTPRDVEEVYQTNVFGIVRMmntFVPLLEKSEQPVVVNVSSGLGSfgmv 142
Cdd:cd05338   84 EATVDQFGRLDILVNNAGaiwLSLVEDTPAK-RFDLMQRVNLRGTYLLSQA---ALPHMVKAGQGHILNISPPLSL---- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 143 tNPetAESKVnslAYCSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDLVGDFSNNSKHVSEGIKP------IIQLA 214
Cdd:cd05338  156 -RP--ARGDV---AYAAGKAGMSRLTLGLAAELrrHGIAVNSLWPSTAIETPAATELSGGSDPARARSPeilsdaVLAIL 229

                        250
                 ....*....|.
gi 446083982 215 TIDADGPTGTF 225
Cdd:cd05338  230 SRPAAERTGLV 240
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 3-192 2.42e-12

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 64.72  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKAL-----GYKVYIGSRNDVRGQQASQKL---------GVHYVQLDVTSDYSVKNAYNMI 68
Cdd:cd08941    2 KVVLVTGANSGLGLAICERLLAEddenpELTLILACRNLQRAEAACRALlashpdarvVFDYVLVDLSNMVSVFAAAKEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  69 AEKEGRLDILINNAGI--------------------------------SGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNT 116
Cdd:cd08941   82 KKRYPRLDYLYLNAGImpnpgidwigaikevltnplfavtnptykiqaEGLLSQGDKATEDGLGEVFQTNVFGHYYLIRE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446083982 117 FVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAESKVNSLAYCSSKSAVTMLTLQYAKGLPNMQINA--ADPGATNTDL 192
Cdd:cd08941  162 LEPLLCRSDGGSQIIWTSSLNASPKYFSLEDIQHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSyvVHPGICTTNL 239
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-140 2.49e-12

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 65.47  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEAL-KALGYKVYIGSR--------NDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:cd08953  209 LVTGGAGGIGRALARALaRRYGARLVLLGRsplppeeeWKAQTLAALEALGarVLYISADVTDAAAVRRLLEKVRERYGA 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446083982  75 LDILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMmntfVPLLEKSEQPVVVNVSSGLGSFG 140
Cdd:cd08953  289 IDGVIHAAGV-LRDALLAQKTAEDFEAVLAPKVDGLLNL----AQALADEPLDFFVLFSSVSAFFG 349
PRK09135 PRK09135
pteridine reductase; Provisional
 1-187 2.85e-12

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 64.18  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRndvRGQQASQKL----------GVHYVQLDVTSDYSVKNAYNMIAE 70
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYH---RSAAEADALaaelnalrpgSAAALQADLLDPDALPELVAACVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  71 KEGRLDILINNAgiSGQFSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNvssglgsfgmVTNPETAE 149
Cdd:PRK09135  82 AFGRLDALVNNA--SSFYPTPlGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVN----------ITDIHAER 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 150 SKVNSLAYCSSKSAVTMLTLQYAKGL-PNMQINAADPGA 187
Cdd:PRK09135 149 PLKGYPVYCAAKAALEMLTRSLALELaPEVRVNAVAPGA 187
PRK07774 PRK07774
SDR family oxidoreductase;
3-191 2.94e-12

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 64.00  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07774   7 KVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadggTAIAVQVDVSDPDSAKAMADATVSAFGGIDY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLT--PRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGlGSFgMVTNPetaeskvnsl 155
Cdd:PRK07774  87 LVNNAAIYGGMKLDLLITvpWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSST-AAW-LYSNF---------- 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446083982 156 aYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTD 191
Cdd:PRK07774 155 -YGLAKVGLNGLTQQLARelGGMNIRVNAIAPGPIDTE 191
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-198 3.86e-12

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 63.97  E-value: 3.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKV---YIGSRNDVRGQQAS-QKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIavnYARSRKAAEETAEEiEALGRkaLAVKANVGDVEKIKEMFAQIDEEFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGiSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGSFGMVTNpetaeskvns 154
Cdd:PRK08063  83 LDVFVNNAA-SGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSS-LGSIRYLEN---------- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446083982 155 laYCS---SKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFSN 198
Cdd:PRK08063 151 --YTTvgvSKAALEALTRYLAVELApkGIAVNAVSGGAVDTDALKHFPN 197
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 3-134 6.00e-12

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 63.77  E-value: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQ-------KLGVHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSrileewhKARVEAMTLDLASLRSVQRFAEAFKAKNSPL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446083982  76 DILINNAGIsgqFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS 134
Cdd:cd09809   82 HVLVCNAAV---FALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSS 137
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 3-192 6.77e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 62.97  E-value: 6.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQ---KLG---VHYVQLDVTSdySVKNAY----NMIAEKE 72
Cdd:PRK08945  13 RIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDeieAAGgpqPAIIPLDLLT--ATPQNYqqlaDTIEEQF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  73 GRLDILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtnpetaesKV 152
Cdd:PRK08945  91 GRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQG----------RA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 153 NSLAYCSSKSAV--TMLTLQYAKGLPNMQINAADPGATNTDL 192
Cdd:PRK08945 161 NWGAYAVSKFATegMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK06123 PRK06123
SDR family oxidoreductase;
1-230 7.44e-12

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 62.87  E-value: 7.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIgsrNDVRGQQASQKL-------GVHY--VQLDVTSDYSVKNAYNMIAEK 71
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCL---NYLRNRDAAEAVvqairrqGGEAlaVAADVADEADVLRLFEAVDRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  72 EGRLDILINNAGISGQFSTPSKLTPRDVEEVYQTNVFG-------IVRMMNTfvplLEKSEQPVVVNVSS---GLGSFGM 141
Cdd:PRK06123  78 LGRLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGsflcareAVKRMST----RHGGRGGAIVNVSSmaaRLGSPGE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 142 VTNpetaeskvnslaYCSSKSAVTMLTLQYAKGLPN--MQINAADPGATNTDL--VGDFSNNSKHVSEGI---------- 207
Cdd:PRK06123 154 YID------------YAASKGAIDTMTIGLAKEVAAegIRVNAVRPGVIYTEIhaSGGEPGRVDRVKAGIpmgrggtaee 221

                        250       260
                 ....*....|....*....|....*
gi 446083982 208 --KPIIQLATIDADGPTGTFINGNG 230
Cdd:PRK06123 222 vaRAILWLLSDEASYTTGTFIDVSG 246
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-191 8.04e-12

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 63.02  E-value: 8.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVH--YVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:cd05363    4 KTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAacAISLDVTDQASIDRCVAALVDRWGSIDILVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsgqFS-TPSKLTPRDV-EEVYQTNVFGIVRMMNTFV-PLLEKSEQPVVVNVSSGLGSFGmvtnpetaESKVNslAY 157
Cdd:cd05363   84 NAAL---FDlAPIVDITRESyDRLFAINVSGTLFMMQAVArAMIAQGRGGKIINMASQAGRRG--------EALVG--VY 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 158 CSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTD 191
Cdd:cd05363  151 CATKAAVISLTQSAGLNLIrhGINVNAIAPGVVDGE 186
PRK06500 PRK06500
SDR family oxidoreductase;
3-194 8.68e-12

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 62.67  E-value: 8.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06500   7 KTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGesALVIRADAGDVAAQKALAQALAEAFGRLDAVFI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGIsgqfstpSKLTP-RDVEE-----VYQTNVFGIVRMMNTFVPLLEKSEQpVVVNVSSGlGSFGMvtnpetaeskVNS 154
Cdd:PRK06500  87 NAGV-------AKFAPlEDWDEamfdrSFNTNVKGPYFLIQALLPLLANPAS-IVLNGSIN-AHIGM----------PNS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446083982 155 LAYCSSKSAVtmltLQYAKGLPN------MQINAADPGATNTDLVG 194
Cdd:PRK06500 148 SVYAASKAAL----LSLAKTLSGellprgIRVNAVSPGPVQTPLYG 189
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 2-163 9.90e-12

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 63.31  E-value: 9.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALG-YKVYIGSRNDVRGQQASQKLGV-----HYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:cd09810    1 KGTVVITGASSGLGLAAAKALARRGeWHVVMACRDFLKAEQAAQEVGMpkdsySVLHCDLASLDSVRQFVDNFRRTGRPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGIsgQFSTPSKL--TPRDVEEVYQTNVFGIVRMMNTFVPLLEKSE--QPVVVNVSSGLGsfgmvtNPETAESK 151
Cdd:cd09810   81 DALVCNAAV--YLPTAKEPrfTADGFELTVGVNHLGHFLLTNLLLEDLQRSEnaSPRIVIVGSITH------NPNTLAGN 152

                        170
                 ....*....|..
gi 446083982 152 VNSLAYCSSKSA 163
Cdd:cd09810  153 VPPRATLGDLEG 164
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-164 1.05e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 63.07  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGgddrVLTVVADVTDLAAMQAAAEEAVERFGGIDVV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVnVSSgLGSFG---MVTnpetaeskvnsl 155
Cdd:PRK05872  90 VANAGIA-SGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQ-VSS-LAAFAaapGMA------------ 154


                 ....*....
gi 446083982 156 AYCSSKSAV 164
Cdd:PRK05872 155 AYCASKAGV 163
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 3-192 1.06e-11

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 62.49  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQ-ASQKLGVHYVQLDVTSDYSVKNAYNMIaekeGRLDILINN 81
Cdd:cd05351    8 KRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSlVRECPGIEPVCVDLSDWDATEEALGSV----GPVDLLVNN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSSGLGSfgmvtnpetaESKVNSLAYCSS 160
Cdd:cd05351   84 AAVA-ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARgMIARGVPGSIVNVSSQASQ----------RALTNHTVYCST 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 161 KSAVTMLTLQYAK--GLPNMQINAADPGATNTDL 192
Cdd:cd05351  153 KAALDMLTKVMALelGPHKIRVNSVNPTVVMTDM 186
PRK08219 PRK08219
SDR family oxidoreductase;
1-192 1.07e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 62.26  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALkALGYKVYIGSRNDVRGQQASQKL-GVHYVQLDVTSDYSVKNAynmiAEKEGRLDILI 79
Cdd:PRK08219   2 ERPTALITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELAAELpGATPFPVDLTDPEAIAAA----VEQLGRLDVLV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVV-VNVSSGLGsfgmvTNPETAeskvnslAYC 158
Cdd:PRK08219  77 HNAGVA-DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVfINSGAGLR-----ANPGWG-------SYA 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 159 SSKSAVTMLtlqyAKGL-----PNMQINAADPGATNTDL 192
Cdd:PRK08219 144 ASKFALRAL----ADALreeepGNVRVTSVHPGRTDTDM 178
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-230 1.14e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 62.50  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGN--KGLGYASAEALKALGYKVY--------------IGSRNDVRGQQASQKLGV--HYVQLDVTSDYSVKNA 64
Cdd:PRK12859   7 KVAVVTGVSrlDGIGAAICKELAEAGADIFftywtaydkempwgVDQDEQIQLQEELLKNGVkvSSMELDLTQNDAPKEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  65 YNMIAEKEGRLDILINNAGIS--GQFSTpskLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMV 142
Cdd:PRK12859  87 LNKVTEQLGYPHILVNNAAYStnNDFSN---LTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 143 TNpetaeskvnsLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVgdfsnnSKHVSEGIKP----------- 209
Cdd:PRK12859 164 GE----------LAYAATKGAIDALTSSLAAEVAHLGItvNAINPGPTDTGWM------TEEIKQGLLPmfpfgrigepk 227

                        250       260
                 ....*....|....*....|....*.
gi 446083982 210 -----IIQLATIDADGPTGTFINGNG 230
Cdd:PRK12859 228 daarlIKFLASEEAEWITGQIIHSEG 253
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-84 2.12e-11

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 61.97  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY-------VQLDVTSDYSVKNAYNMIAEKEG 73
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgegmaygFGADATSEQSVLALSRGVDEIFG 80

                         90
                 ....*....|.
gi 446083982  74 RLDILINNAGI 84
Cdd:PRK12384  81 RVDLLVYNAGI 91
PRK07577 PRK07577
SDR family oxidoreductase;
3-216 2.36e-11

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 61.28  E-value: 2.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRN---DVRGQqasqklgvhYVQLDVTSDYSVKNAYNMIAEKeGRLDILI 79
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSaidDFPGE---------LFACDLADIEQTAATLAQINEI-HPVDAIV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGSFGMvtnpetaeskVNSLAYCS 159
Cdd:PRK07577  74 NNVGIA-LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICS-RAIFGA----------LDRTSYSA 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446083982 160 SKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLvgdFSNNSKHVSEGIKPIiqLATI 216
Cdd:PRK07577 142 AKSALVGCTRTWALELAEYGItvNAVAPGPIETEL---FRQTRPVGSEEEKRV--LASI 195
PRK07035 PRK07035
SDR family oxidoreductase;
3-201 2.63e-11

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 61.57  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNdVRGQQA-----------SQKLGVHYVQLDvtsdySVKNAYNMIAEK 71
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRK-LDGCQAvadaivaaggkAEALACHIGEME-----QIDALFAHIRER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  72 EGRLDILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmvtnpetaesk 151
Cdd:PRK07035  83 HGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVAS----------------- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446083982 152 VNSLA-------YCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDLVGDFSNNSK 201
Cdd:PRK07035 146 VNGVSpgdfqgiYSITKAAVISMTKAFAKecAPFGIRVNALLPGLTDTKFASALFKNDA 204
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-186 2.73e-11

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 61.84  E-value: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK08277  11 KVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKaaggeALAVKADVLDKESLEQARQQILEDFGPCDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAG--------ISGQFSTPS------KLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgMvt 143
Cdd:PRK08277  91 LINGAGgnhpkattDNEFHELIEptktffDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISS------M-- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 144 NPETAESKVnsLAYCSSKSAVTMLTLQYAKGL--PNMQINAADPG 186
Cdd:PRK08277 163 NAFTPLTKV--PAYSAAKAAISNFTQWLAVHFakVGIRVNAIAPG 205
PRK05717 PRK05717
SDR family oxidoreductase;
3-186 5.65e-11

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 60.67  E-value: 5.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVH--YVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENawFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAGISGQFSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLeKSEQPVVVNVSSglgsfgmvtnPETAESKVNSLAYCS 159
Cdd:PRK05717  91 NAAIADPHNTTlESLSLAHWNRVLAVNLTGPMLLAKHCAPYL-RAHNGAIVNLAS----------TRARQSEPDTEAYAA 159

                        170       180
                 ....*....|....*....|....*...
gi 446083982 160 SKSAVTMLTLQYAKGL-PNMQINAADPG 186
Cdd:PRK05717 160 SKGGLLALTHALAISLgPEIRVNAVSPG 187
PRK06139 PRK06139
SDR family oxidoreductase;
3-161 6.13e-11

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 60.89  E-value: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQ---KLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK06139   8 AVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecrALGaeVLVVPTDVTDADQVKALATQAASFGGRIDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGIS--GQFSTpsklTPRDV-EEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGSFgmVTNPETAeskvns 154
Cdd:PRK06139  88 WVNNVGVGavGRFEE----TPIEAhEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMIS-LGGF--AAQPYAA------ 154


                 ....*..
gi 446083982 155 lAYCSSK 161
Cdd:PRK06139 155 -AYSASK 160
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 5-192 6.47e-11

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 59.84  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAynmiAEKEGRLDILINNAGI 84
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPADVAAELEVWAL----AQELGPLDLLVYAAGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  85 SGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfgmVTNPETAeskvnslAYCSSKSAV 164
Cdd:cd11730   77 ILG-KPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPEL-----VMLPGLS-------AYAAAKAAL 143

                        170       180
                 ....*....|....*....|....*...
gi 446083982 165 TMLTLQYAKGLPNMQINAADPGATNTDL 192
Cdd:cd11730  144 EAYVEVARKEVRGLRLTLVRPPAVDTGL 171
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 3-164 7.55e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 60.71  E-value: 7.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL---GVH--YVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07109   9 QVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraaGGEalAVVADVADAEAVQAAADRAEEELGPIDT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMvtnPETAeskvnslAY 157
Cdd:PRK07109  89 WVNNAMVT-VFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSI---PLQS-------AY 157


                 ....*..
gi 446083982 158 CSSKSAV 164
Cdd:PRK07109 158 CAAKHAI 164
PRK05855 PRK05855
SDR family oxidoreductase;
3-167 7.66e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 61.15  E-value: 7.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQ---ASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK05855 316 KLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERtaeLIRAAGAvaHAYRVDVSDADAMEAFAEWVRAEHGVPDI 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGI--SGQF-STPskltPRDVEEVYQTNVFGIV-------RMMntfvplLEKSEQPVVVNVSSGlgsfgmvtnpeT 147
Cdd:PRK05855 396 VVNNAGIgmAGGFlDTS----AEDWDRVLDVNLWGVIhgcrlfgRQM------VERGTGGHIVNVASA-----------A 454

                        170       180
                 ....*....|....*....|.
gi 446083982 148 AESKVNSL-AYCSSKSAVTML 167
Cdd:PRK05855 455 AYAPSRSLpAYATSKAAVLML 475
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 1-186 8.46e-11

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 59.95  E-value: 8.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06483   1 MPAPILITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGAQCIQADFSTNAGIMAFIDELKQHTDGLRAIIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  81 NAgiSGQFSTPSKLTPRDVeevyqtnvfgIVRMMNTFV-----------PLLEKSEQPV--VVNVSSglgsfgmvtnpET 147
Cdd:PRK06483  81 NA--SDWLAEKPGAPLADV----------LARMMQIHVnapyllnlaleDLLRGHGHAAsdIIHITD-----------YV 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446083982 148 AE--SKvNSLAYCSSKSAVTMLTLQYAKGL-PNMQINAADPG 186
Cdd:PRK06483 138 VEkgSD-KHIAYAASKAALDNMTLSFAAKLaPEVKVNSIAPA 178
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 3-132 8.92e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 60.06  E-value: 8.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-GVHYVQLDVTS-DYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK06125   8 KRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLrAAHGVDVAVHAlDLSSPEAREQLAAEAGDIDILVN 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446083982  81 NAG-ISGqfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNV 132
Cdd:PRK06125  88 NAGaIPG--GGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV 138
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 3-219 1.01e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 60.20  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-------VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK05875   8 RTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEalkgagaVRYEPADVTDEDQVARAVDAATAWHGRL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISgqfSTPSKLTPRDVEEVYQT---NVFGIVRmmntfvpLLEKSEQPVvvnVSSGLGSFgmVTNPETAESKV 152
Cdd:PRK05875  88 HGVVHCAGGS---ETIGPITQIDSDAWRRTvdlNVNGTMY-------VLKHAAREL---VRGGGGSF--VGISSIAASNT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446083982 153 NSL--AYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDLVGdfsnnskhvsegikPIIQLATIDAD 219
Cdd:PRK05875 153 HRWfgAYGVTKSAVDHLMKLAADelGPSWVRVNSIRPGLIRTDLVA--------------PITESPELSAD 209
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 3-186 1.42e-10

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 59.78  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd08935    6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITalggrAIALAADVLDRASLERAREEIVAQFGTVDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAG-------------ISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmvTN 144
Cdd:cd08935   86 LINGAGgnhpdattdpehyEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISS--------MN 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446083982 145 PETAESKVnsLAYCSSKSAVTMLTLQYAK--GLPNMQINAADPG 186
Cdd:cd08935  158 AFSPLTKV--PAYSAAKAAVSNFTQWLAVefATTGVRVNAIAPG 199
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 4-139 1.63e-10

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 59.00  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINN 81
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGdnLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446083982  82 AGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSF 139
Cdd:PRK10538  82 AGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSW 139
PRK09009 PRK09009
SDR family oxidoreductase;
5-234 1.64e-10

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 58.92  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKA--LGYKVYIGSRNDVRGQQASqklGVHYVQLDVTSDYSVKNaynmIAEKEGRLDILINNA 82
Cdd:PRK09009   3 ILIVGGSGGIGKAMVKQLLEryPDATVHATYRHHKPDFQHD---NVQWHALDVTDEAEIKQ----LSEQFTQLDWLINCV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIsgqFSTPSKLTPRDVE----EVYQTNVfgivrMMNT---------FVPLLEKSEQPVVVNVSSGLGSfgmVTNpetae 149
Cdd:PRK09009  76 GM---LHTQDKGPEKSLQaldaDFFLQNI-----TLNTlpslllakhFTPKLKQSESAKFAVISAKVGS---ISD----- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 150 skvNSL----AYCSSKSAVTM----LTLQYAKGLPNMQINAADPGATNTDLVGDFSNN--------SKHVSEGIKPIIQL 213
Cdd:PRK09009 140 ---NRLggwySYRASKAALNMflktLSIEWQRSLKHGVVLALHPGTTDTALSKPFQQNvpkgklftPEYVAQCLLGIIAN 216

                        250       260
                 ....*....|....*....|..
gi 446083982 214 ATIDAdgpTGTFINGNGE-MPW 234
Cdd:PRK09009 217 ATPAQ---SGSFLAYDGEtLPW 235
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 2-219 1.70e-10

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 59.43  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   2 TKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL--GVHYVQLDVTSDYSVKNaynmIAEKE---GRLD 76
Cdd:cd08951    7 MKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACpgAAGVLIGDLSSLAETRK----LADQVnaiGRFD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGIsgqFSTPSKLTPRDveevyqtnvfGIVRM--MNTFVP--LLEKSEQP-VVVNVSSGLGSFGMVTNPETAESK 151
Cdd:cd08951   83 AVIHNAGI---LSGPNRKTPDT----------GIPAMvaVNVLAPyvLTALIRRPkRLIYLSSGMHRGGNASLDDIDWFN 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446083982 152 V---NSLAYCSSKSAVTMLTLQYAKGLPNMQINAADPGATNTDLVGdfSNNSKHVSEGIKPIIQLATIDAD 219
Cdd:cd08951  150 RgenDSPAYSDSKLHVLTLAAAVARRWKDVSSNAVHPGWVPTKMGG--AGAPDDLEQGHLTQVWLAESDDP 218
PRK08589 PRK08589
SDR family oxidoreductase;
3-200 3.58e-10

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 58.64  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQ--QASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK08589   7 KVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSEtvDKIKSNGgkAKAYHVDISDEQQVKDFASEIKEQFGRVDVL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLtPRDV-EEVYQTNVFGIVRMMNTFVPLLEKsEQPVVVNVSSGLGSfgmvtnpetaESKVNSLAY 157
Cdd:PRK08589  87 FNNAGVDNAAGRIHEY-PVDVfDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQ----------AADLYRSGY 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446083982 158 CSSKSAVTMLT----LQYAKglPNMQINAADPGATNTDLVGDFSNNS 200
Cdd:PRK08589 155 NAAKGAVINFTksiaIEYGR--DGIRANAIAPGTIETPLVDKLTGTS 199
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
1-193 3.76e-10

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 58.10  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTK-IVLITGGNKGLGYASAEALKALGYKVYIG----SRNDVRGQQASQKLGVHYV--QLDVTSDYSVKNAYNMIAEKEG 73
Cdd:PRK12938   1 MSQrIAYVTGGMGGIGTSICQRLHKDGFKVVAGcgpnSPRRVKWLEDQKALGFDFIasEGNVGDWDSTKAAFDKVKAEVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  74 RLDILINNAGISGQFsTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSS---GLGSFGMvTNPETAES 150
Cdd:PRK12938  81 EIDVLVNNAGITRDV-VFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSvngQKGQFGQ-TNYSTAKA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 151 KVNSLAYCSSKSAVTmltlqyaKGLpnmQINAADPGATNTDLV 193
Cdd:PRK12938 159 GIHGFTMSLAQEVAT-------KGV---TVNTVSPGYIGTDMV 191
PRK06482 PRK06482
SDR family oxidoreductase;
1-137 4.74e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 58.20  E-value: 4.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYigsrNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVA----ATVRRPDALDDLKARYgdrlwvLQLDVTDSAAVRAVVDRAFAALGR 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446083982  75 LDILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLG 137
Cdd:PRK06482  77 IDVVVSNAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGG 138
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 3-205 6.60e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 57.74  E-value: 6.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKV---YIGSRNDVR-GQQASQKLGVHYVQL--DVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEGADIaivYLDEHEDANeTKQRVEKEGVKCLLIpgDVSDEAFCKDAVEETVRELGRLD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEqpVVVNVSSGLGSFGmvtNPETaeskvnsLA 156
Cdd:PRK06701 127 ILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGS--AIINTGSITGYEG---NETL-------ID 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPN--MQINAADPGATNTDLV-GDFSnnSKHVSE 205
Cdd:PRK06701 195 YSATKGAIHAFTRSLAQSLVQkgIRVNAVAPGPIWTPLIpSDFD--EEKVSQ 244
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 3-199 7.88e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 57.25  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07478   7 KVAIITGASSGIGRAAAKLFAREGAKVVVGARrqaelDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLG-SFGMvtnPETAeskvnslA 156
Cdd:PRK07478  87 AFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGhTAGF---PGMA-------A 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 157 YCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDLVGDFSNN 199
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAeyGAQGIRVNALLPGGTDTPMGRAMGDT 201
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 3-193 1.06e-09

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 56.92  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKV---YIGSRNDV--RGQQASQKLGVHYVQL--DVTSDYSVKNAYNMIAEKEGRL 75
Cdd:cd05355   27 KKALITGGDSGIGRAVAIAFAREGADVainYLPEEEDDaeETKKLIEEEGRKCLLIpgDLGDESFCRDLVKEVVKEFGKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEqpVVVNVSSGLGSFGmvtNPETaeskvnsL 155
Cdd:cd05355  107 DILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKGS--SIINTTSVTAYKG---SPHL-------L 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 156 AYCSSKSA-VTM---LTLQYA-KGLpnmQINAADPGATNTDLV 193
Cdd:cd05355  175 DYAATKGAiVAFtrgLSLQLAeKGI---RVNAVAPGPIWTPLI 214
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-175 1.10e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 57.02  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIG-SRNDVRGQQASQKLGVHY--VQLDVTSDYSVKnayNMIAEKEGR--- 74
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVNyHQSEDAAEALADELGDRAiaLQADVTDREQVQ---AMFATATEHfgk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 -LDILINNAGISGQFSTPSKLTPRDVE-EVYQTNVFGIVR----MMNTFVPLLEKSEQPVVVNVSSGLgsfgmVTNPeta 148
Cdd:PRK08642  81 pITTVVNNALADFSFDGDARKKADDITwEDFQQQLEGSVKgalnTIQAALPGMREQGFGRIINIGTNL-----FQNP--- 152

                        170       180
                 ....*....|....*....|....*..
gi 446083982 149 esKVNSLAYCSSKSAVTMLTLQYAKGL 175
Cdd:PRK08642 153 --VVPYHDYTTAKAALLGLTRNLAAEL 177
PRK12743 PRK12743
SDR family oxidoreductase;
1-194 1.15e-09

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 56.97  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS----QKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETaeevRSHGVraEIRQLDLSDLPEGAQALDKLIQRLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGiSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQP-VVVNVSSglgsfgmvTNPETAesKVN 153
Cdd:PRK12743  81 IDVLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGgRIINITS--------VHEHTP--LPG 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 154 SLAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVG 194
Cdd:PRK12743 150 ASAYTAAKHALGGLTKAMALELVehGILVNAVAPGAIATPMNG 192
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-187 1.26e-09

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 56.56  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIgsrNDVRGQQASQKLGVHYVQLDV----------TSDY-SVKNAYNMIA-- 69
Cdd:cd05353    6 RVVLVTGAGGGLGRAYALAFAERGAKVVV---NDLGGDRKGSGKSSSAADKVVdeikaaggkaVANYdSVEDGEKIVKta 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  70 -EKEGRLDILINNAGI--SGQFstpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVtnpe 146
Cdd:cd05353   83 iDAFGRVDILVNNAGIlrDRSF---AKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNF---- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446083982 147 taeSKVNslaYCSSKSAVTMLTLQYAKGLP--NMQINAADPGA 187
Cdd:cd05353  156 ---GQAN---YSAAKLGLLGLSNTLAIEGAkyNITCNTIAPAA 192
PRK07831 PRK07831
SDR family oxidoreductase;
3-137 1.31e-09

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 56.58  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGG-NKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-------VHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK07831  18 KVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAaelglgrVEAVVCDVTSEAQVDALIDAAVERLGR 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446083982  75 LDILINNAGISGQFSTpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQP-VVVNVSSGLG 137
Cdd:PRK07831  98 LDVLVNNAGLGGQTPV-VDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGgVIVNNASVLG 160
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 3-190 1.79e-09

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 56.39  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVR-----GQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGlattvKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSkLTPRDVEEVYQTNVFGIVRMMNTFVPL--LEKSEQPVVVNVSSGLGSFGMvtnpetaeskVNSL 155
Cdd:cd08945   84 LVNNAGRSGGGATAE-LADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGV----------VHAA 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 156 AYCSSKSAVTMLT----LQYAKglPNMQINAADPGATNT 190
Cdd:cd08945  153 PYSASKHGVVGFTkalgLELAR--TGITVNAVCPGFVET 189
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 4-228 2.00e-09

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 56.05  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKVYiGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNAG 83
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVV-CHDASFADAAERQAFESENPGTKALSEQKPEELVDAVLQAGGAIDVLVSNDY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  84 ISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvnslAYCSSKSA 163
Cdd:cd05361   82 IPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNS----------LYGPARAA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446083982 164 VTMLTLQYAKGLP--NMQINAADPGATNTDL---VGDFSNNSKHVSEGIK--PIIQLATIDADGPTGTFING 228
Cdd:cd05361  152 AVALAESLAKELSrdNILVYAIGPNFFNSPTyfpTSDWENNPELRERVKRdvPLGRLGRPDEMGALVAFLAS 223
PRK05866 PRK05866
SDR family oxidoreductase;
3-165 2.04e-09

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 56.29  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK05866  41 KRILLTGASSGIGEAAAEQFARRGATVVAVARredllDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTP-RDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPvVVNVSsglgSFGMvtnpeTAESKVNSL 155
Cdd:PRK05866 121 LINNAGRSIRRPLAESLDRwHDVERTMVLNYYAPLRLIRGLAPgMLERGDGH-IINVA----TWGV-----LSEASPLFS 190

                        170
                 ....*....|
gi 446083982 156 AYCSSKSAVT 165
Cdd:PRK05866 191 VYNASKAALS 200
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-176 2.20e-09

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.14  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAynmiaekEGRLDILINNAGI 84
Cdd:COG0451    2 ILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAA-------LAGVDAVVHLAAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  85 SGqfstpskLTPRDVEEVYQTNVFGIVRMMNtfvpLLEKSEQPVVVNVSSGlGSFGMVTNP--ETAESKVNSlAYCSSKS 162
Cdd:COG0451   75 AG-------VGEEDPDETLEVNVEGTLNLLE----AARAAGVKRFVYASSS-SVYGDGEGPidEDTPLRPVS-PYGASKL 141

                        170
                 ....*....|....*.
gi 446083982 163 AVTMLTLQYAK--GLP 176
Cdd:COG0451  142 AAELLARAYARryGLP 157
PRK05867 PRK05867
SDR family oxidoreductase;
3-193 3.12e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 55.43  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsggKVVPVCCDVSQHQQVTSMLDQVTAELGGIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGI---SGQFSTPSKltprDVEEVYQTNVFGIvrmmntFVplleKSEQPVVVNVSSGLGSfGMVTNPETAESKVNS 154
Cdd:PRK05867  90 AVCNAGIitvTPMLDMPLE----EFQRLQNTNVTGV------FL----TAQAAAKAMVKQGQGG-VIINTASMSGHIINV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 155 LA----YCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTDLV 193
Cdd:PRK05867 155 PQqvshYCASKAAVIHLTKAMAVELAphKIRVNSVSPGYILTELV 199
PRK07024 PRK07024
SDR family oxidoreductase;
1-164 4.64e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 54.94  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKV-YIGSRNDV-RGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK07024   1 MPLKVFITGASSGIGQALAREYARQGATLgLVARRTDAlQAFAARLPKAarVSVYAADVRDADALAAAAADFIAAHGLPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTpSKLTPRDV-EEVYQTNVFGivrMMNTFVPLLE---KSEQPVVVNVSSGLGSFGMvtnPETAeskv 152
Cdd:PRK07024  81 VVIANAGISVGTLT-EEREDLAVfREVMDTNYFG---MVATFQPFIApmrAARRGTLVGIASVAGVRGL---PGAG---- 149

                        170
                 ....*....|..
gi 446083982 153 nslAYCSSKSAV 164
Cdd:PRK07024 150 ---AYSASKAAA 158
PRK07775 PRK07775
SDR family oxidoreductase;
5-190 6.86e-09

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 54.76  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQK--------LGVHyvqLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKiradggeaVAFP---LDVTDPDSVKSFVAQAEEALGEIE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGiSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfGMVTNPETAeskvnslA 156
Cdd:PRK07775  90 VLVSGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDV---ALRQRPHMG-------A 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPNMQINAA--DPGATNT 190
Cdd:PRK07775 159 YGAAKAGLEAMVTNLQMELEGTGVRASivHPGPTLT 194
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-158 1.83e-08

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 53.36  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINkaggkAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGI----------------------SGQFSTpsklTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSG 135
Cdd:PRK13394  88 LVSNAGIqivnpienysfadwkkmqaihvDGAFLT----TKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHG 163

                        170       180
                 ....*....|....*....|...
gi 446083982 136 LGSFGMVTNPETAESKVNSLAYC 158
Cdd:PRK13394 164 LLGLARVLAKEGAKHNVRSHVVC 186
PRK06194 PRK06194
hypothetical protein; Provisional
 3-168 2.32e-08

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 53.10  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGsrnDVRG---QQASQKLG-----VHYVQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVLA---DVQQdalDRAVAELRaqgaeVLGVRTDVSDAAQVEALADAALERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGI-SGQFSTPSklTPRDVEEVYQTNVFGIVRMMNTFVPL-LEKSEQPV-----VVNVSSGLGSFgmvtNPET 147
Cdd:PRK06194  84 VHLLFNNAGVgAGGLVWEN--SLADWEWVLGVNLWGVIHGVRAFTPLmLAAAEKDPayeghIVNTASMAGLL----APPA 157

                        170       180
                 ....*....|....*....|.
gi 446083982 148 AEskvnslAYCSSKSAVTMLT 168
Cdd:PRK06194 158 MG------IYNVSKHAVVSLT 172
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 3-189 2.35e-08

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 53.02  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSR----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK12823   9 KVVVVTGAAQGIGRGVALRAAAEGARVVLVDRselvHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDVL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmvtnpeTAESKVNSLAYC 158
Cdd:PRK12823  89 INNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSS------------IATRGINRVPYS 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 159 SSKSAVTMLT----LQYAKGlpNMQINAADPGATN 189
Cdd:PRK12823 157 AAKGGVNALTaslaFEYAEH--GIRVNAVAPGGTE 189
PRK05854 PRK05854
SDR family oxidoreductase;
3-192 5.09e-08

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 52.38  E-value: 5.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL-------GVHYVQLDVTSDYSVKnAYNMIAEKEGR- 74
Cdd:PRK05854  15 KRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIrtavpdaKLSLRALDLSSLASVA-ALGEQLRAEGRp 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  75 LDILINNAGIsgqFSTPSKLTPRDVEEV-YQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAESKVN 153
Cdd:PRK05854  94 IHLLINNAGV---MTPPERQTTADGFELqFGTNHLGHFALTAHLLPLLRAGRARVTSQSSIAARRGAINWDDLNWERSYA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446083982 154 SL-AYCSSKSAVTMLTLQY-----AKGLPNMQiNAADPGATNTDL 192
Cdd:PRK05854 171 GMrAYSQSKIAVGLFALELdrrsrAAGWGITS-NLAHPGVAPTNL 214
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-191 6.55e-08

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.83  E-value: 6.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYK-VYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:PRK12481   9 KVAIITGCNTGLGQGMAIGLAKAGADiVGVGVAEAPETQAQVEALGrkFHFITADLIQQKDIDSIVSQAVEVMGHIDILI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  80 NNAGISG-----QFSTPSKltpRDVEEVYQTNVFGIVR-MMNTFVpllEKSEQPVVVNVSSGLGSFGMVTNPetaeskvn 153
Cdd:PRK12481  89 NNAGIIRrqdllEFGNKDW---DDVININQKTVFFLSQaVAKQFV---KQGNGGKIINIASMLSFQGGIRVP-------- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 154 slAYCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNTD 191
Cdd:PRK12481 155 --SYTASKSAVMGLTRALATELSqyNINVNAIAPGYMATD 192
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 4-109 1.14e-07

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 50.84  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   4 IVLITGGNKGLGYASAEALKALGYKV-YIGSRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVaLAARREAKLEALLVDIIrdaggSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446083982  78 LINNAGiSGQFSTPSKLTPRDVEEVYQTNVFG 109
Cdd:cd05373   81 LVYNAG-ANVWFPILETTPRVFEKVWEMAAFG 111
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-192 1.23e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 50.87  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK06077   7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENggegigVLADVSTREGCETLAKATIDRYGVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEksEQPVVVNVSSGLGSFGMVTNPetaeskvnslA 156
Cdd:PRK06077  87 ILVNNAGL-GLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMR--EGGAIVNIASVAGIRPAYGLS----------I 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446083982 157 YCSSKSAVTMLTLQYAKGL-PNMQINAADPGATNTDL 192
Cdd:PRK06077 154 YGAMKAAVINLTKYLALELaPKIRVNAIAPGFVKTKL 190
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-230 2.17e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 50.14  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRND---VRGQQASQKLG-VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNEnklKRMKKTLSKYGnIHYVVGDVSSTESARNVIEKAAKVLNAIDGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAG--ISGQFSTPSKLtprdvEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmvtnpeTAESkvNSLA 156
Cdd:PRK05786  86 VVTVGgyVEDTVEEFSGL-----EEMLTNHIKIPLYAVNASLRFLKEGSSIVLVSSMSGIY---------KASP--DQLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 157 YCSSKSAVTMLTLQYAKGLPN--MQINAADPGATNTDLV--GDFSNNSKHVSEGIKP------IIQLATIDADGPTGTFI 226
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGrgIRVNGIAPTTISGDFEpeRNWKKLRKLGDDMAPPedfakvIIWLLTDEADWVDGVVI 229


                 ....
gi 446083982 227 NGNG 230
Cdd:PRK05786 230 PVDG 233
PRK08340 PRK08340
SDR family oxidoreductase;
5-83 2.27e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 50.19  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL----GVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELkeygEVYAVKADLSDKDDLKNLVKEAWELLGGIDALVW 82


                 ...
gi 446083982  81 NAG 83
Cdd:PRK08340  83 NAG 85
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 5-109 3.85e-07

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 48.63  E-value: 3.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982     5 VLITGGNKGLGYASAEALKALGY-KVYIGSRNDVRGQQASQKLG--------VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAeleaagarVTVVACDVADRDALAAVLAAIPAVEGPL 82

                           90       100       110
                   ....*....|....*....|....*....|....
gi 446083982    76 DILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFG 109
Cdd:smart00822  83 TGVIHAAGV-LDDGVLASLTPERFAAVLAPKAAG 115
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 3-79 4.80e-07

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 49.25  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITG--GNKGLGYASAEALKALGYKVYIGSRNDVRG---QQASQKLGVHYV-QLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:COG0623    6 KRGLITGvaNDRSIAWGIAKALHEEGAELAFTYQGEALKkrvEPLAEELGSALVlPCDVTDDEQIDALFDEIKEKWGKLD 85


                 ...
gi 446083982  77 ILI 79
Cdd:COG0623   86 FLV 88
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 6-232 5.32e-07

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 49.14  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG--VHYVQLDVTSDYSVKnAYNMIAEKE-GRLDILINNA 82
Cdd:PRK12936  10 LVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGerVKIFPANLSDRDEVK-ALGQKAEADlEGVDILVNNA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  83 GIS--GQFstpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGmvtNPETAEskvnslaYCSS 160
Cdd:PRK12936  89 GITkdGLF---VRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTG---NPGQAN-------YCAS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 161 KSAVTMLTLQYAKGLP--NMQINAADPGATNTDLVGDFSNNSKHVSEGIKP-------------IIQLATIDADGPTGTF 225
Cdd:PRK12936 156 KAGMIGFSKSLAQEIAtrNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPmkrmgtgaevasaVAYLASSEAAYVTGQT 235


                 ....*..
gi 446083982 226 INGNGEM 232
Cdd:PRK12936 236 IHVNGGM 242
PRK12746 PRK12746
SDR family oxidoreductase;
3-230 7.58e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 48.49  E-value: 7.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIG-SRNDVRGQQASQKL-----GVHYVQLDVTSDYSVKNAYNMIAEK----- 71
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIesnggKAFLIEADLNSIDGVKKLVEQLKNElqirv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  72 -EGRLDILINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQpvVVNVSSGLGSFGMvtnpetaes 150
Cdd:PRK12746  87 gTSEIDILVNNAGIGTQ-GTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGR--VINISSAEVRLGF--------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 151 kVNSLAYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDL---------VGDFSNNSK------HVSEGIKPIIQL 213
Cdd:PRK12746 155 -TGSIAYGLSKGALNTMTLPLAKhlGERGITVNTIMPGYTKTDInakllddpeIRNFATNSSvfgrigQVEDIADAVAFL 233

                        250
                 ....*....|....*..
gi 446083982 214 ATIDADGPTGTFINGNG 230
Cdd:PRK12746 234 ASSDSRWVTGQIIDVSG 250
PRK09134 PRK09134
SDR family oxidoreductase;
1-188 1.04e-06

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 48.39  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKV---YIGSRNDVR---------GQQAsqklgvHYVQLDVTSDYSVKNAYNMI 68
Cdd:PRK09134   8 APRAALVTGAARRIGRAIALDLAAHGFDVavhYNRSRDEAEalaaeiralGRRA------VALQADLADEAEVRALVARA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  69 AEKEGRLDILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVssglgsfgmvtnpetA 148
Cdd:PRK09134  82 SAALGPITLLVNNASLF-EYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNM---------------I 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446083982 149 ESKVNSL-----AYCSSKSAVTMLTLQYAKGL-PNMQINAADPGAT 188
Cdd:PRK09134 146 DQRVWNLnpdflSYTLSKAALWTATRTLAQALaPRIRVNAIGPGPT 191
PRK06128 PRK06128
SDR family oxidoreductase;
6-192 1.09e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 48.32  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIG--------SRNDVRGQQASQKLGVHyVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK06128  59 LITGADSGIGRATAIAFAREGADIALNylpeeeqdAAEVVQLIQAEGRKAVA-LPGDLKDEAFCRQLVERAVKELGGLDI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQpvVVNVSSglgsfgmvtnPETAESKVNSLAY 157
Cdd:PRK06128 138 LVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGAS--IINTGS----------IQSYQPSPTLLDY 205

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446083982 158 CSSKSAVTMLTLQYAKGL--PNMQINAADPGATNTDL 192
Cdd:PRK06128 206 ASTKAAIVAFTKALAKQVaeKGIRVNAVAPGPVWTPL 242
PRK07023 PRK07023
SDR family oxidoreductase;
6-192 1.11e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 48.09  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVtSDysVKNAYNMIAEKEGRLD-------IL 78
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSLAAAAGERLAEVELDL-SD--AAAAAAWLAGDLLAAFvdgasrvLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmvtNPETAESkvnslAYC 158
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAAR-----NAYAGWS-----VYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446083982 159 SSKSAVTMLTLQYAK-GLPNMQINAADPGATNTDL 192
Cdd:PRK07023 152 ATKAALDHHARAVALdANRALRIVSLAPGVVDTGM 186
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 3-177 1.62e-06

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 47.32  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYigsrndVRGQQASQKLGVHYVQLDVTSDY-SVKNAYNMIAEKEGRLDILINN 81
Cdd:cd05334    2 RVVLVYGGRGALGSAVVQAFKSRGWWVA------SIDLAENEEADASIIVLDSDSFTeQAKQVVASVARLSGKVDALICV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  82 AGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGL-GSFGMVtnpetaeskvnslAYCSS 160
Cdd:cd05334   76 AGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALePTPGMI-------------GYGAA 142

                        170       180
                 ....*....|....*....|
gi 446083982 161 KSAVTMLTLQYA---KGLPN 177
Cdd:cd05334  143 KAAVHQLTQSLAaenSGLPA 162
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 3-102 2.04e-06

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 47.67  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYvqldvTSDysvknayNMIAEKEGrlDILInna 82
Cdd:PRK08655   1 MKISIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEY-----AND-------NIDAAKDA--DIVI--- 63

                         90       100
                 ....*....|....*....|
gi 446083982  83 gisgqFSTPSKLTPRDVEEV 102
Cdd:PRK08655  64 -----ISVPINVTEDVIKEV 78
PRK12742 PRK12742
SDR family oxidoreductase;
3-107 2.48e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 47.06  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKV---YIGSRNdvRGQQASQKLGVHYVQLDVTSdysvKNAYNMIAEKEGRLDILI 79
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDGANVrftYAGSKD--AAERLAQETGATAVQTDSAD----RDAVIDVVRKSGALDILV 80

                         90       100
                 ....*....|....*....|....*...
gi 446083982  80 NNAGIsGQFSTPSKLTPRDVEEVYQTNV 107
Cdd:PRK12742  81 VNAGI-AVFGDALELDADDIDRLFKINI 107
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-85 2.68e-06

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 47.07  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY------VQLDVTSDYSVKNAYNMIAEKEGR 74
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYgekaygFGADATNEQSVIALSKGVDEIFKR 80

                         90
                 ....*....|.
gi 446083982  75 LDILINNAGIS 85
Cdd:cd05322   81 VDLLVYSAGIA 91
PRK07806 PRK07806
SDR family oxidoreductase;
3-82 2.87e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 2.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDV-RGQQASQKL---GVH--YVQLDVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK07806   7 KTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKApRANKVVAEIeaaGGRasAVGADLTDEESVAALMDTAREEFGGLD 86


                 ....*.
gi 446083982  77 ILINNA 82
Cdd:PRK07806  87 ALVLNA 92
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-84 3.84e-06

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 47.14  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVyIGSrnDVRGQQAS-----QKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAHV-VCL--DVPAAGEAlaavaNRVGGTALALDITAPDAPARIAEHLAERHGGLDI 287


                 ....*..
gi 446083982  78 LINNAGI 84
Cdd:PRK08261 288 VVHNAGI 294
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-210 6.06e-06

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 46.31  E-value: 6.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIgsrNDV---------------RGQQASQKLGvhyvqlDVtSDYSVKNAYNM 67
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVV---NDVasaldasdvldeiraAGAKAVAVAG------DI-SQRATADELVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  68 IAEKEGRLDILINNAGISGQ---FSTpSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQ-PV---VVNVSSGLGSFG 140
Cdd:PRK07792  83 TAVGLGGLDIVVNNAGITRDrmlFNM-SDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKAAGgPVygrIVNTSSEAGLVG 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446083982 141 MVTNPEtaeskvnslaYCSSKSAVTMLTLQYAKGLPNMQI--NAADPGATNTDLVGDFSNNSKHVSEGIKPI 210
Cdd:PRK07792 162 PVGQAN----------YGAAKAGITALTLSAARALGRYGVraNAICPRARTAMTADVFGDAPDVEAGGIDPL 223
PRK07074 PRK07074
SDR family oxidoreductase;
1-190 7.79e-06

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 45.53  E-value: 7.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   1 MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG---VHYVQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGdarFVPVACDLTDAASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGiSGQFSTPSKLTPrdveEVYQT----NVFGIVRMMNTFVPLLEKSEQPVVVNVSS--GLGSFGmvtNPETAESK 151
Cdd:PRK07074  81 LVANAG-AARAASLHDTTP----ASWRAdnalNLEAAYLCVEAVLEGMLKRSRGAVVNIGSvnGMAALG---HPAYSAAK 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 152 VNSLAYCSSksavtmLTLQYAKGlpNMQINAADPGATNT 190
Cdd:PRK07074 153 AGLIHYTKL------LAVEYGRF--GIRANAVAPGTVKT 183
PRK08278 PRK08278
SDR family oxidoreductase;
3-172 8.06e-06

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 45.66  E-value: 8.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDvrgqQASQKL-GVHY---------------VQLDVTSDYSVKNAYN 66
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGANIVIAAKTA----EPHPKLpGTIHtaaeeieaaggqalpLVGDVRDEDQVAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  67 MIAEKEGRLDILINNAG---ISGQFSTPSKltpR-DVeeVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLgsfgmV 142
Cdd:PRK08278  83 KAVERFGGIDICVNNASainLTGTEDTPMK---RfDL--MQQINVRGTFLVSQACLPHLKKSENPHILTLSPPL-----N 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 446083982 143 TNPETAESKVnslAYCSSKSAVTMLTLQYA 172
Cdd:PRK08278 153 LDPKWFAPHT---AYTMAKYGMSLCTLGLA 179
PRK07985 PRK07985
SDR family oxidoreductase;
6-192 1.08e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 45.37  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIgSRNDVRGQQASQ------KLGVHYVQL--DVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07985  53 LVTGGDSGIGRAAAIAYAREGADVAI-SYLPVEEEDAQDvkkiieECGRKAVLLpgDLSDEKFARSLVHEAHKALGGLDI 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQpvVVNVSSglgsfgmvtnPETAESKVNSLAY 157
Cdd:PRK07985 132 MALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGAS--IITTSS----------IQAYQPSPHLLDY 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 158 CSSKSAVtmltLQYAKGLPN------MQINAADPGATNTDL 192
Cdd:PRK07985 200 AATKAAI----LNYSRGLAKqvaekgIRVNIVAPGPIWTAL 236
PRK09186 PRK09186
flagellin modification protein A; Provisional
 3-186 1.14e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 44.98  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY-------VQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK09186   5 KTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFkskklslVELDITDQESLEEFLSKSAEKYGKI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNA-GISGQFSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmVTNP--ETAE-- 149
Cdd:PRK09186  85 DGAVNCAyPRNKDYGKKfFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYG----VVAPkfEIYEgt 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446083982 150 SKVNSLAYCSSKSAVTMLTLQYAKGLPNMQI--NAADPG 186
Cdd:PRK09186 161 SMTSPVEYAAIKAGIIHLTKYLAKYFKDSNIrvNCVSPG 199
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-187 1.27e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 45.05  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIgsrNDVRGQQASQKLGVHYVQLDV-------------TSDYS-VKNAYNMI 68
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVV---NDIGVGLDGSASGGSAAQAVVdeivaaggeavanGDDIAdWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  69 A---EKEGRLDILINNAGI--SGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPV---VVNVSSGLGSFG 140
Cdd:PRK07791  84 DaavETFGGLDVLVNNAGIlrDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAESKAGRAVdarIINTSSGAGLQG 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446083982 141 MVtnpetaeSKVNslaYCSSKSAVTMLTLQYAKGLPN--MQINAADPGA 187
Cdd:PRK07791 164 SV-------GQGN---YSAAKAGIAALTLVAAAELGRygVTVNAIAPAA 202
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-226 1.30e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 45.07  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALG--YKVYIGSRNDvrgqqaSQKLGVHYVQLDVTSDYS----------VKNAYNMIAE 70
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGalVAIHYGNRKE------EAEETVYEIQSNGGSAFSiganleslhgVEALYSSLDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  71 K------EGRLDILINNAGIsGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQpvVVNVSSGlgsfgmvtn 144
Cdd:PRK12747  79 ElqnrtgSTKFDILINNAGI-GPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR--IINISSA--------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982 145 pETAESKVNSLAYCSSKSAVTMLTLQYAK--GLPNMQINAADPGATNTDLVGDFSNNS--KHVSEGIKPIIQLATIDADG 220
Cdd:PRK12747 147 -ATRISLPDFIAYSMTKGAINTMTFTLAKqlGARGITVNAILPGFIKTDMNAELLSDPmmKQYATTISAFNRLGEVEDIA 225


                 ....*.
gi 446083982 221 PTGTFI 226
Cdd:PRK12747 226 DTAAFL 231
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 3-190 1.41e-05

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 44.84  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYsVKNA------YNMIAEKEGRLD 76
Cdd:cd08936   11 KVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCH-VGKAedrerlVATAVNLHGGVD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSgLGSFgmvtNPETAESkvnslA 156
Cdd:cd08936   90 ILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSS-VAAF----HPFPGLG-----P 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446083982 157 YCSSKSAVTMLTLQYAKGLP--NMQINAADPGATNT 190
Cdd:cd08936  160 YNVSKTALLGLTKNLAPELAprNIRVNCLAPGLIKT 195
PRK08703 PRK08703
SDR family oxidoreductase;
3-190 2.71e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 43.77  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNdVRGQQASQKLGVH-------YVQLDVTSdySVKNAYNMIA-----E 70
Cdd:PRK08703   7 KTILVTGASQGLGEQVAKAYAAAGATVILVARH-QKKLEKVYDAIVEaghpepfAIRFDLMS--AEEKEFEQFAatiaeA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  71 KEGRLDILINNAgisGQFSTPSKLTPRDVEE---VYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgsfgmvTNPET 147
Cdd:PRK08703  84 TQGKLDGIVHCA---GYFYALSPLDFQTVAEwvnQYRINTVAPMGLTRALFPLLKQSPDASVIFVGE--------SHGET 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446083982 148 AESKVNslAYCSSKSAVTMLTLQYA---KGLPNMQINAADPGATNT 190
Cdd:PRK08703 153 PKAYWG--GFGASKAALNYLCKVAAdewERFGNLRANVLVPGPINS 196
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 3-79 4.18e-05

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 43.34  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITG--GNKGLGYASAEALKALGYKVYIGSRNDV---RGQQASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:cd05372    2 KRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPEAlrkRVEKLAERLGEsaLVLPCDVSNDEEIKELFAEVKKDWGKL 81


                 ....
gi 446083982  76 DILI 79
Cdd:cd05372   82 DGLV 85
PRK06114 PRK06114
SDR family oxidoreductase;
3-190 5.78e-05

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 42.85  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQAS----QKLGVHYVQL--DVTSDYSVKNAYNMIAEKEGRLD 76
Cdd:PRK06114   9 QVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETaehiEAAGRRAIQIaaDVTSKADLRAAVARTEAELGALT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGqfSTPS-KLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSfgmVTNPETAESKVNsl 155
Cdd:PRK06114  89 LAVNAAGIAN--ANPAeEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGI---IVNRGLLQAHYN-- 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 156 aycSSKSAVTMLTLQYA-----KGLpnmQINAADPGATNT 190
Cdd:PRK06114 162 ---ASKAGVIHLSKSLAmewvgRGI---RVNSISPGYTAT 195
PLN00015 PLN00015
protochlorophyllide reductase
 6-84 5.96e-05

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 43.16  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALG-YKVYIGSRNDVRGQQASQKLGV---HYV--QLDVTSDYSVKNAYNMIAEKEGRLDILI 79
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGkWHVVMACRDFLKAERAAKSAGMpkdSYTvmHLDLASLDSVRQFVDNFRRSGRPLDVLV 80


                 ....*
gi 446083982  80 NNAGI 84
Cdd:PLN00015  81 CNAAV 85
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-186 6.77e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 43.02  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHY-----VQLDVTSDYSVKNAYNMIAEKEGRLDI 77
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGpeglgVSADVRDYAAVEAAFAQIADEFGPIDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  78 LInnAGISGQFSTPS-KLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSeQPVVVNVSSGLGsfgmvTNPETAESKVnsla 156
Cdd:PRK07576  90 LV--SGAAGNFPAPAaGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRP-GASIIQISAPQA-----FVPMPMQAHV---- 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446083982 157 yCSSKSAVTMLT--LQYAKGLPNMQINAADPG 186
Cdd:PRK07576 158 -CAAKAGVDMLTrtLALEWGPEGIRVNSIVPG 188
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
19-196 1.09e-04

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 42.30  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  19 AEALKALGYKVyIGSrnDVRGQQasqkLGVH-YVQLDVTSDYSVKNAynmIAEKEGRLDILINNAGISGQFstpskltpr 97
Cdd:PRK12428   2 ARLLRFLGARV-IGV--DRREPG----MTLDgFIQADLGDPASIDAA---VAALPGRIDALFNIAGVPGTA--------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  98 DVEEVYQTNVFGIVRMMNTFVPLLekSEQPVVVNVSSGLGSfGMVTNPETAESKVNS------LAYCS------------ 159
Cdd:PRK12428  63 PVELVARVNFLGLRHLTEALLPRM--APGGAIVNVASLAGA-EWPQRLELHKALAATasfdegAAWLAahpvalatgyql 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446083982 160 SKSAVTMLTLQYAKGL---PNMQINAADPGATNTDLVGDF 196
Cdd:PRK12428 140 SKEALILWTMRQAQPWfgaRGIRVNCVAPGPVFTPILGDF 179
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-189 1.31e-04

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 41.78  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVyIGSrNDVRGQQASQK---LGVHYVqlDVTSDYSVKNAYNMIAEKE----GRL 75
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGCDI-VGI-NIVEPTETIEQvtaLGRRFL--SLTADLRKIDGIPALLERAvaefGHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQfSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSSGLGSFGMVTNPetaeskvns 154
Cdd:PRK08993  87 DILVNNAGLIRR-EDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKhFIAQGNGGKIINIASMLSFQGGIRVP--------- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446083982 155 lAYCSSKSAVTMLTL----QYAKGlpNMQINAADPG--ATN 189
Cdd:PRK08993 157 -SYTASKSGVMGVTRlmanEWAKH--NINVNAIAPGymATN 194
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 5-102 3.02e-04

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 41.22  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYK-VYIGSRN--DVRGQQASQKLG-----VHYVQLDVTSDYSVKNAYnMIAEKEGRLD 76
Cdd:cd05274  153 YLITGGLGGLGLLVARWLAARGARhLVLLSRRgpAPRAAARAALLRaggarVSVVRCDVTDPAALAALL-AELAAGGPLA 231

                         90       100
                 ....*....|....*....|....*.
gi 446083982  77 ILINNAGIsGQFSTPSKLTPRDVEEV 102
Cdd:cd05274  232 GVIHAAGV-LRDALLAELTPAAFAAV 256
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 3-117 3.42e-04

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 41.22  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVY-IGSRND-VRGQQASQKLGVHYVQldvtsdYSVKNAYNMIAEKEgRLDILIN 80
Cdd:PRK07424 179 KTVAVTGASGTLGQALLKELHQQGAKVVaLTSNSDkITLEINGEDLPVKTLH------WQVGQEAALAELLE-KVDILII 251

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446083982  81 NAGISgqfsTPSKLTPRDVEEVYQTNVFGIVRMMNTF 117
Cdd:PRK07424 252 NHGIN----VHGERTPEAINKSYEVNTFSAWRLMELF 284
PRK08416 PRK08416
enoyl-ACP reductase;
3-198 3.81e-04

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 40.52  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKV-YIGSRN----DVRGQQASQKLGV--HYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:PRK08416   9 KTLVISGGTRGIGKAIVYEFAQSGVNIaFTYNSNveeaNKIAEDLEQKYGIkaKAYPLNILEPETYKELFKKIDEDFDRV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  76 DILINNAGISGQ-----FSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSglgSFGMVTNPetaes 150
Cdd:PRK08416  89 DFFISNAIISGRavvggYTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSS---TGNLVYIE----- 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446083982 151 kvNSLAYCSSKSAV-TMltLQYAK---GLPNMQINAADPGATNTDLVGDFSN 198
Cdd:PRK08416 161 --NYAGHGTSKAAVeTM--VKYAAtelGEKNIRVNAVSGGPIDTDALKAFTN 208
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 3-172 4.44e-04

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 40.12  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDV----------RGQQASQKLGVHYVQL--DVTSDYSVKNAYNMIAE 70
Cdd:cd09762    4 KTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiyTAAEEIEAAGGKALPCivDIRDEDQVRAAVEKAVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  71 KEGRLDILINNAG---ISGQFSTPSKltprDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGsfgmvTNPET 147
Cdd:cd09762   84 KFGGIDILVNNASaisLTGTLDTPMK----RYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLN-----LNPKW 154

                        170       180
                 ....*....|....*....|....*
gi 446083982 148 AEskvNSLAYCSSKSAVTMLTLQYA 172
Cdd:cd09762  155 FK---NHTAYTMAKYGMSMCVLGMA 176
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 5-141 4.56e-04

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 39.85  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982    5 VLITGGNKGLGYASAEALKALGYK--VYIGSRNDVRGQQAS-----QKLG--VHYVQLDVTSDYSVKNAYNMIAEKEGRL 75
Cdd:pfam08659   3 YLITGGLGGLGRELARWLAERGARhlVLLSRSAAPRPDAQAliaelEARGveVVVVACDVSDPDAVAALLAEIKAEGPPI 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446083982   76 DILINNAGISgQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFvpllekSEQPV--VVNVSSGLGSFGM 141
Cdd:pfam08659  83 RGVIHAAGVL-RDALLENMTDEDWRRVLAPKVTGTWNLHEAT------PDEPLdfFVLFSSIAGLLGS 143
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 6-141 5.02e-04

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 40.32  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQA-----SQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILIN 80
Cdd:PRK05876  10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAvnhlrAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFS 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446083982  81 NAGISgqFSTP-SKLTPRDVEEVYQTNVFGIVRMMNTFVP-LLEKSEQPVVVNVSS--------GLGSFGM 141
Cdd:PRK05876  90 NAGIV--VGGPiVEMTHDDWRWVIDVDLWGSIHTVEAFLPrLLEQGTGGHVVFTASfaglvpnaGLGAYGV 158
PRK07041 PRK07041
SDR family oxidoreductase;
6-61 7.71e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 39.64  E-value: 7.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   6 LITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLG----VHYVQLDVTSDYSV 61
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGggapVRTAALDITDEAAV 60
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 6-101 1.14e-03

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 39.14  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982    6 LITGGNKGLGYASAEALKALGYKVYIGSRNDvrgQQASQKLGVHY----------VQLDVTSDYSVKNAYNMIAEKE--- 72
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRS---AAAASTLAAELnarrpnsavtCQADLSNSATLFSRCEAIIDACfra 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 446083982   73 -GRLDILINNAgiSGQFSTPskLTPRDVEE 101
Cdd:TIGR02685  82 fGRCDVLVNNA--SAFYPTP--LLRGDAGE 107
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
3-79 1.17e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 38.94  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNK-GLGYASAEALKALGYKVYIGSRNDvRGQQASQKLG---VHYVQLDVTSDYSVKNAYNMIAEKEGRLDIL 78
Cdd:PRK06079   9 KIVVMGVANKrSIAWGCAQAIKDQGATVIYTYQND-RMKKSLQKLVdeeDLLVECDVASDESIERAFATIKERVGKIDGI 87


                 .
gi 446083982  79 I 79
Cdd:PRK06079  88 V 88
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 5-83 1.26e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.23  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNkGLGYASAEALKALGYKVYIGSRNDVRGQQAsQKLGVHYVqldvtSDYSVKNAYNMIAEKEGR-LDILINNAG 83
Cdd:cd05188  138 VLVLGAG-GVGLLAAQLAKAAGARVIVTDRSDEKLELA-KELGADHV-----IDYKEEDLEEELRLTGGGgADVVIDAVG 210
PRK07102 PRK07102
SDR family oxidoreductase;
3-177 1.65e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 38.75  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKL------GVHYVQLDVTsDYSVKNAynMIAEKEGRLD 76
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrargavAVSTHELDIL-DTASHAA--FLDSLPALPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  77 ILINNAGISGQfstpSKLTPRDVEE---VYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNpetaeskvn 153
Cdd:PRK07102  79 IVLIAVGTLGD----QAACEADPALalrEFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASN--------- 145

                        170       180
                 ....*....|....*....|....
gi 446083982 154 sLAYCSSKSAVTmltlQYAKGLPN 177
Cdd:PRK07102 146 -YVYGSAKAALT----AFLSGLRN 164
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 5-98 1.82e-03

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 38.33  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRNDVRgqqasqklgvhyVQLDVTSDYSVKNAYnmiaEKEGRLDILINNAGi 84
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGD------------YQVDITDEASIKALF----EKVGHFDAIVSTAG- 63

                         90
                 ....*....|....
gi 446083982  85 SGQFSTPSKLTPRD 98
Cdd:cd11731   64 DAEFAPLAELTDAD 77
PRK06101 PRK06101
SDR family oxidoreductase;
5-192 2.00e-03

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 38.31  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVYIGSRN-DVRGQQASQKLGVHYVQLDVTSDYSVKNAynmIAEKEGRLDILINNAG 83
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNqSVLDELHTQSANIFTLAFDVTDHPGTKAA---LSQLPFIPELWIFNAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  84 iSGQFSTPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVnvssglGSFGMVTNPETAEskvnslAYCSSKSA 163
Cdd:PRK06101  81 -DCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGHRVVIV------GSIASELALPRAE------AYGASKAA 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446083982 164 VTML--TLQY---AKGLpnmQINAADPGATNTDL 192
Cdd:PRK06101 148 VAYFarTLQLdlrPKGI---EVVTVFPGFVATPL 178
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 3-81 2.91e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 38.06  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNdVRGQQASQ--------------KLGVH--YVQLDVTSDYSVKNAYN 66
Cdd:PRK08303   9 KVALVAGATRGAGRGIAVELGAAGATVYVTGRS-TRARRSEYdrpetieetaelvtAAGGRgiAVQVDHLVPEQVRALVE 87

                         90
                 ....*....|....*
gi 446083982  67 MIAEKEGRLDILINN 81
Cdd:PRK08303  88 RIDREQGRLDILVND 102
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
 5-176 4.24e-03

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 37.58  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   5 VLITGGNKGLGYASAEALKALGYKVY-IGSR-----NDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIaekegRLDIL 78
Cdd:cd05260    2 ALITGITGQDGSYLAEFLLEKGYEVHgIVRRsssfnTDRIDHLYINKDRITLHYGDLTDSSSLRRAIEKV-----RPDEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982  79 INNAGISgqFSTPSKLTPrdvEEVYQTNVFGIVRMMNTfvpLLEKSEQPVVVNVSSGlGSFGMVtnPETAESKVNSL--- 155
Cdd:cd05260   77 YHLAAQS--HVKVSFDDP---EYTAEVNAVGTLNLLEA---IRILGLDARFYQASSS-EEYGKV--QELPQSETTPFrpr 145

                        170       180
                 ....*....|....*....|..
gi 446083982 156 -AYCSSKSAVTMLTLQYAKGLP 176
Cdd:cd05260  146 sPYAVSKLYADWITRNYREAYG 167
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 5-135 4.49e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 37.28  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982    5 VLITGGNKGLGYASAEALKALGYKVYIGSRnDVRGQQASQKLGVHYVQLDVTSDYSVKNaynmiAEKEGRLDILINNAGI 84
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDR-LTSASNTARLADLRFVEGDLTDRDALEK-----LLADVRPDAVIHLAAV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446083982   85 SG---QFSTPskltprdvEEVYQTNVFGIVRMMNtfvpLLEKSEQPVVVNVSSG 135
Cdd:pfam01370  75 GGvgaSIEDP--------EDFIEANVLGTLNLLE----AARKAGVKRFLFASSS 116
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
3-93 5.49e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 37.00  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITG--GNKGLGYASAEALKALGYKVYIGSRNDVRG------QQASQKLGVH-YVQLDVTSDYSVKNAYNMIAEKEG 73
Cdd:PRK07370   7 KKALVTGiaNNRSIAWGIAQQLHAAGAELGITYLPDEKGrfekkvRELTEPLNPSlFLPCDVQDDAQIEETFETIKQKWG 86

                         90       100
                 ....*....|....*....|....*.
gi 446083982  74 RLDILI------NNAGISGQFSTPSK 93
Cdd:PRK07370  87 KLDILVhclafaGKEELIGDFSATSR 112
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 3-84 8.61e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 36.53  E-value: 8.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASqKLGVHYVQldVTSDYSVKnaynmiAEKEGRLDILINNA 82
Cdd:cd08259  164 DTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILK-ELGADYVI--DGSKFSED------VKKLGGADVVIELV 234


                 ..
gi 446083982  83 GI 84
Cdd:cd08259  235 GS 236
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 3-133 9.16e-03

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 36.43  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446083982   3 KIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRgqQASQKLGVHYVqldvtSDYSVKNAYNMIaEKEGRLDILINNA 82
Cdd:cd08248  164 KRVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDAI--PLVKSLGADDV-----IDYNNEDFEEEL-TERGKFDVILDTV 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446083982  83 GISGQFSTPSKLTPRDV------EEVYQTNVFGIVR-MMNTFVPLLEKSEQPVVVNVS 133
Cdd:cd08248  236 GGDTEKWALKLLKKGGTyvtlvsPLLKNTDKLGLVGgMLKSAVDLLKKNVKSLLKGSH 293
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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